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- Author:
- Micsonai, András; Wien, Frank; Kernya, Linda; Lee, Young-Ho; Goto, Yuji; Ráéfráéégiers, Matthieu; Kardos, Jáééózsef
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2015 v.112 no.24 pp. E3095
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; X-radiation; amyloid; circular dichroism spectroscopy; nuclear magnetic resonance spectroscopy; prediction; topology; Show all 7 Subjects
- Abstract:
- ... Circular dichroism (CD) spectroscopy is a widely used technique for the study of protein structure. Numerous algorithms have been developed for the estimation of the secondary structure composition from the CD spectra. These methods often fail to provide acceptable results on α/β-mixed or β-structure–rich proteins. The problem arises from the spectral diversity of β-structures, which has hitherto ...
- DOI:
- 10.1073/pnas.1500851112
- PubMed:
- 26038575
- PubMed Central:
- PMC4475991
- http://dx.doi.org/10.1073/pnas.1500851112
- Author:
- Tsutsui, Yuko; Dela Cruz, Richard; Wintrode, Patrick L.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2012 v.109 no.12 pp. 4467-4472
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; genetic disorders; humans; mass spectrometry; polymerization; protein folding; proteinases; Show all 7 Subjects
- Abstract:
- ... The misfolding of serpins is linked to several genetic disorders including emphysema, thrombosis, and dementia. During folding, inhibitory serpins are kinetically trapped in a metastable state in which a stretch of residues near the C terminus of the molecule are exposed to solvent as a flexible loop (the reactive center loop). When they inhibit target proteases, serpins transition to a stable sta ...
- DOI:
- 10.1073/pnas.1109125109
- PubMed:
- 22392975
- PubMed Central:
- PMC3311335
- http://dx.doi.org/10.1073/pnas.1109125109
- Author:
- Moran, Sean D.; Woys, Ann Marie; Buchanan, Lauren E.; Bixby, Eli; Decatur, Sean M.; Zanni, Martin T.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2012 v.109 no.9 pp. 3329-3334
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; amyloid; carbon; cataract; crystallins; eye lens; humans; infrared spectroscopy; isotope dilution technique; isotope labeling; models; stable isotopes; Show all 12 Subjects
- Abstract:
- ... The structural eye lens protein γD-crystallin is a major component of cataracts, but its conformation when aggregated is unknown. Using expressed protein ligation, we uniformly 13C labeled one of the two Greek key domains so that they are individually resolved in two-dimensional (2D) IR spectra for structural and kinetic analysis. Upon acid-induced amyloid fibril formation, the 2D IR spectra reve ...
- DOI:
- 10.1073/pnas.1117704109
- PubMed:
- 22328156
- PubMed Central:
- PMC3295317
- http://dx.doi.org/10.1073/pnas.1117704109
- Author:
- Westfield, Gerwin H.; Rasmussen, Søren G. F.; Su, Min; Dutta, Somnath; DeVree, Brian T.; Chung, Ka Young; Calinski, Diane; Velez-Ruiz, Gisselle; Oleskie, Austin N.; Pardon, Els; Chae, Pil Seok; Liu, Tong; Li, Sheng; Woods, Virgil L., Jr.; Steyaert, Jan; Kobilka, Brian K.; Sunahara, Roger K.; Skiniotis, Georgios
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2011 v.108 no.38 pp. 16086-16091
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; G-proteins; adrenergic receptors; beta-adrenergic agonists; crystal structure; electron microscopy; guanosine diphosphate; molecular models; Show all 8 Subjects
- Abstract:
- ... The active-state complex between an agonist-bound receptor and a guanine nucleotide-free G protein represents the fundamental signaling assembly for the majority of hormone and neurotransmitter signaling. We applied single-particle electron microscopy (EM) analysis to examine the architecture of agonist-occupied β2-adrenoceptor (β2AR) in complex with the heterotrimeric G protein Gs (Gαsβγ). EM 2D ...
- DOI:
- 10.1073/pnas.1113645108
- PubMed:
- 21914848
- PubMed Central:
- PMC3179071
- http://dx.doi.org/10.1073/pnas.1113645108
- Author:
- Spåhr, Henrik; Calero, Guillermo; Bushnell, David A.; Kornberg, Roger D.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2009 v.106 no.23 pp. 9185-9190
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Schizosaccharomyces pombe; DNA-directed RNA polymerase; crystal structure; X-ray diffraction; Show all 5 Subjects
- Abstract:
- ... The second structure of a eukaryotic RNA polymerase II so far determined, that of the enzyme from the fission yeast Schizosaccharomyces pombe, is reported here. Comparison with the previous structure of the enzyme from the budding yeast Saccharomyces cerevisiae reveals differences in regions implicated in start site selection and transcription factor interaction. These aspects of the transcription ...
- DOI:
- 10.1073/pnas.0903361106
- PubMed:
- 19458260
- PubMed Central:
- PMC2684843
- http://dx.doi.org/10.1073/pnas.0903361106
- Author:
- Zhang, Xing; Boyce, Mark; Bhattacharya, Bishnupriya; Zhang, Xiaokang; Schein, Stan; Roy, Polly; Zhou, Z. Hong
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2010 v.107 no.14 pp. 6292-6297
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; coat proteins; sialic acids; Bluetongue virus; electron microscopy; binding proteins; binding sites; viral morphology; Show all 8 Subjects
- Abstract:
- ... Bluetongue virus (BTV) is transmitted by blood-feeding insects (Culicoides sp.) and causes hemorrhagic diseases in livestock. BTV is a nonenveloped, double-stranded RNA (dsRNA) virus with two capsids: a well-studied, stable core enclosing the dsRNA genome and a highly unstable, poorly studied coat responsible for host cell attachment and entry. Here, based on cryo-electron microscopy (cryoEM), we ...
- DOI:
- 10.1073/pnas.0913403107
- PubMed:
- 20332209
- PubMed Central:
- PMC2852009
- http://dx.doi.org/10.1073/pnas.0913403107
- Author:
- Chang, Hsiang-Yu; Lin, Jia-Yu; Lee, Han-Chung; Wang, Hui-Ling; King, Chih-Yen
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2008 v.105 no.36 pp. 13345-13350
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; protein aggregates; yeasts; Saccharomyces cerevisiae; fungal proteins; nucleotide sequences; amyloid; prions; Show all 8 Subjects
- Abstract:
- ... Amyloid polymorphism underlies the prion strain phenomenon where a single protein polypeptide adopts different chain-folding patterns to form self-propagating cross-β structures. Three strains of the yeast prion [PSI], namely [VH], [VK], and [VL], have been previously characterized and are amyloid conformers of the yeast translation termination factor Sup35. Here we define specific sequences of th ...
- DOI:
- 10.1073/pnas.0802215105
- PubMed:
- 18757753
- PubMed Central:
- PMC2533192
- http://dx.doi.org/10.1073/pnas.0802215105
- Author:
- Murashko, Oleg N.; Kaberdin, Vladimir R.; Lin-Chao, Sue
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2012 v.109 no.18 pp. 7019-7024
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Aquifex; Escherichia coli; Haemophilus influenzae; RNA; Synechocystis; active sites; amino acids; cell membranes; circular dichroism spectroscopy; cooling; deoxyribonuclease I; dissociation; electrostatic interactions; enzyme activity; phospholipids; proteins; ribonucleases; surface area; Show all 19 Subjects
- Abstract:
- ... RNase E plays an essential role in RNA processing and decay and tethers to the cytoplasmic membrane in Escherichia coli; however, the function of this membrane–protein interaction has remained unclear. Here, we establish a mechanistic role for the RNase E–membrane interaction. The reconstituted highly conserved N-terminal fragment of RNase E (NRne, residues 1–499) binds specifically to anionic pho ...
- DOI:
- 10.1073/pnas.1120181109
- PubMed:
- 22509045
- PubMed Central:
- PMC3344982
- http://dx.doi.org/10.1073/pnas.1120181109
- Author:
- Elfrink, Kerstin; Ollesch, Julian; Stöhr, Jan; Willbold, Dieter; Riesner, Detlev; Gerwert, Klaus
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2008 v.105 no.31 pp. 10815-10819
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Fourier transform infrared spectroscopy; PrPC proteins; humans; lipids; post-translational modification; prion diseases; protein binding; protein folding; Show all 9 Subjects
- Abstract:
- ... Misfolding and subsequent aggregation of endogeneous proteins constitute essential steps in many human disorders, including Alzheimer and prion diseases. In most prion protein-folding studies, the posttranslational modifications, the lipid anchor in particular, were lacking. Here, we studied a fully posttranslationally modified cellular prion protein, carrying two N-glycosylations and the natural ...
- DOI:
- 10.1073/pnas.0804721105
- PubMed:
- 18669653
- PubMed Central:
- PMC2504809
- http://dx.doi.org/10.1073/pnas.0804721105
- Author:
- Shewmaker, F.; Wickner, R.B.; Tycko, R.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2006 v.103 no.52 pp. 19754-19759
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Saccharomyces cerevisiae; yeasts; fungal proteins; prions; nuclear magnetic resonance spectroscopy; Show all 6 Subjects
- Abstract:
- ... The [PSI⁺] prion of Saccharomyces cerevisiae is a self-propagating amyloid form of Sup35p, a subunit of the translation termination factor. Using solid-state NMR we have examined the structure of amyloid fibrils formed in vitro from purified recombinant Sup35¹⁻²⁵³, consisting of the glutamine- and asparagine-rich N-terminal 123-residue prion domain (N) and the adjacent 130-residue highly charged M ...
- DOI:
- 10.1073/pnas.0609638103
- PubMed:
- 17170131
- PubMed Central:
- PMC1750918
- http://dx.doi.org/10.1073/pnas.0609638103
- Author:
- Kwan, A.H.Y.; Winefield, R.D.; Sunde, M.; Matthews, J.M.; Haverkamp, R.G.; Templeton, M.D.; Mackay, J.P.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2006 v.103 no.10 pp. 3621-3626
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; X-ray diffraction; Neurospora crassa; nuclear magnetic resonance spectroscopy; fungal proteins; protein secretion; Show all 6 Subjects
- Abstract:
- ... Class I hydrophobins are a unique family of fungal proteins that form a polymeric, water-repellent monolayer on the surface of structures such as spores and fruiting bodies. Similar monolayers are being discovered on an increasing range of important microorganisms. Hydrophobin monolayers are amphipathic and particularly robust, and they reverse the wettability of the surface on which they are form ...
- DOI:
- 10.1073/pnas.0505704103
- PubMed:
- 16537446
- PubMed Central:
- PMC1533775
- http://dx.doi.org/10.1073/pnas.0505704103
- Author:
- Park, Y.J.; Luger, K.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2006 v.103 no.5 pp. 1248-1253
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; nucleosomes; histones; yeasts; Saccharomyces cerevisiae; binding proteins; molecular chaperones; Show all 7 Subjects
- Abstract:
- ... Nucleosome assembly protein 1 (NAP-1) is an integral component in the establishment, maintenance, and dynamics of eukaryotic chromatin. It shuttles histones into the nucleus, assembles nucleosomes, and promotes chromatin fluidity, thereby affecting the transcription of many genes. The 3.0 angstrom crystal structure of yeast NAP-1 reveals a previously uncharacterized fold with implications for hist ...
- DOI:
- 10.1073/pnas.0508002103
- PubMed:
- 16432217
- PubMed Central:
- PMC1345705
- http://dx.doi.org/10.1073/pnas.0508002103
- Author:
- Diaz-Avalos, R.; King, C.Y.; Wall, J.; Simon, M.; Caspar, D.L.D.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2005 v.102 no.29 pp. 10165-10170
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; electron microscopy; yeasts; Saccharomyces cerevisiae; fungal proteins; amyloid; strains; prions; Show all 8 Subjects
- Abstract:
- ... Mass per length (mpl) measurements on single amyloid fibrils that specifically propagate the [VH], [VK], and [VL] strains of the yeast prion [PSI] reveal unanticipated differences in their structures. Many fibrils have approximately equal to 1.0 prion molecule per 4.7-angstrom cross-beta repeat period, which is consistent with a self-replicating model built by parallel beta-sheet hydrogen-bonding ...
- DOI:
- 10.1073/pnas.0504599102
- PubMed:
- 16006506
- PubMed Central:
- PMC1177419
- http://dx.doi.org/10.1073/pnas.0504599102
- Author:
- Anderson, L.K.; Royer, S.M.; Page, S.L.; McKim, K.S.; Lai, A.; Lilly, M.A.; Hawley, R.S.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2005 v.102 no.12 pp. 4482-4487
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; nucleoproteins; synaptonemal complex; immunocytochemistry; Drosophila melanogaster; genetic recombination; Show all 6 Subjects
- Abstract:
- ... The synaptonemal complex (SC) is intimately involved in the process of meiotic recombination in most organisms, but its exact role remains enigmatic. One reason for this uncertainty is that the overall structure of the SC is evolutionarily conserved, but many SC proteins are not. Two putative SC proteins have been identified in Drosophila: C(3)G and C(2)M. Mutations in either gene cause defects in ...
- DOI:
- 10.1073/pnas.0500172102
- PubMed:
- 15767569
- PubMed Central:
- PMC555515
- http://dx.doi.org/10.1073/pnas.0500172102
- Author:
- Calderone, V.; Dolderer, B.; Hartmann, H.J.; Echner, H.; Luchinat, C.; Del Bianco, C.; Mangani, S.; Weser, U.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2005 v.102 no.1 pp. 51-56
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; X-ray diffraction; Saccharomyces cerevisiae; yeasts; metallothionein; crystal structure; copper; Show all 7 Subjects
- Abstract:
- ... We report here the crystal structure of yeast copper thionein (Cu-MT), determined at 1.44-A resolution. The Cu-MT structure shows the largest known oligonuclear Cu(I) thiolate cluster in biology, consisting of six trigonally and two digonally coordinated Cu(I) ions. This is at variance with the results from previous spectroscopic determinations, which were performed on MT samples containing seven ...
- DOI:
- 10.1073/pnas.0408254101
- PubMed:
- 15613489
- PubMed Central:
- PMC544076
- http://dx.doi.org/10.1073/pnas.0408254101
- Author:
- Yennawar, N.H.; Li, L.C.; Dudzinski, D.M.; Tabuchi, A.; Cosgrove, D.J.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2006 v.103 no.40 pp. 14664-14671
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Zea mays; X-ray diffraction; xylan; crystal structure; cell walls; corn; allergens; expansins; pollen; binding capacity; Show all 11 Subjects
- Abstract:
- ... Expansins are small extracellular proteins that promote turgor-driven extension of plant cell walls. EXPB1 (also called Zea m 1) is a member of the β-expansin subfamily known in the allergen literature as group-1 grass pollen allergens. EXPB1 induces extension and stress relaxation of grass cell walls. To help elucidate expansin's mechanism of wall loosening, we determined the structure of EXPB1 b ...
- DOI:
- 10.1073/pnas.0605979103
- PubMed:
- 16984999
- PubMed Central:
- PMC1595409
- http://dx.doi.org/10.1073/pnas.0605979103
- Author:
- Kerff, Frédéric; Amoroso, Ana; Herman, Raphaël; Sauvage, Eric; Petrella, Stéphanie; Filée, Patrice; Charlier, Paulette; Joris, Bernard; Tabuchi, Akira; Nikolaidis, Nikolas; Cosgrove, Daniel J.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2008 v.105 no.44 pp. 16876-16881
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; coleoptiles; bacterial colonization; crystal structure; cell walls; wheat; cellulose; expansins; bacterial proteins; Bacillus subtilis; Triticum aestivum; binding capacity; roots; Show all 13 Subjects
- Abstract:
- ... We solved the crystal structure of a secreted protein, EXLX1, encoded by the yoaJ gene of Bacillus subtilis. Its structure is remarkably similar to that of plant β-expansins (group 1 grass pollen allergens), consisting of 2 tightly packed domains (D1, D2) with a potential polysaccharide-binding surface spanning the 2 domains. Domain D1 has a double-ψ β-barrel fold with partial conservation of the ...
- DOI:
- 10.1073/pnas.0809382105
- PubMed:
- 18971341
- PubMed Central:
- PMC2579346
- http://dx.doi.org/10.1073/pnas.0809382105
- Author:
- Lysek, D.A.; Schorn, C.; Nivon, L.G.; Esteve-Moya, V.; Christen, B.; Calzolai, L.; Schroetter, C. von.; Fiorito, F.; Herrmann, T.; Guntert, P.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2005 v.102 no.3 pp. 640-645
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; prions; nuclear magnetic resonance spectroscopy; cats; dogs; swine; sheep; protein isoforms; amino acid sequences; sequence alignment; Show all 10 Subjects
- Abstract:
- ... The NMR structures of the recombinant cellular form of the prion proteins (PrP(C)) of the cat (Felis catus), dog (Canis familiaris), and pig (Sus scrofa), and of two polymorphic forms of the prion protein from sheep (Ovis aries) are presented. In all of these species, PrP(C) consists of an N-terminal flexibly extended tail with approximately 100 amino acid residues and a C-terminal globular domain ...
- DOI:
- 10.1073/pnas.0408937102
- PubMed:
- 15647367
- PubMed Central:
- PMC545531
- http://dx.doi.org/10.1073/pnas.0408937102
- Author:
- Calzolai, L.; Lysek, D.A.; Perez, D.R.; Guntert, P.; Wuthrich, K.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2005 v.102 no.3 pp. 651-655
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; prions; nuclear magnetic resonance spectroscopy; chickens; Trachemys scripta; turtles; Xenopus laevis; amino acid sequences; Show all 8 Subjects
- Abstract:
- ... The NMR structures of the recombinant prion proteins from chicken (Gallus gallus; chPrP), the red-eared slider turtle (Trachemys scripta; tPrP), and the African clawed frog (Xenopus laevis; xlPrP) are presented. The amino acid sequences of these prion proteins show approximately 30% identity with mammalian prion proteins. All three species form the same molecular architecture as mammalian PrP(C), ...
- DOI:
- 10.1073/pnas.0408939102
- PubMed:
- 15647366
- PubMed Central:
- PMC545536
- http://dx.doi.org/10.1073/pnas.0408939102
20. The molecular structure of spider dragline silk: folding and orientation of the protein backbone
- Author:
- Beek, J.D. van.; Hess, S.; Vollrath, F.; Meier, B.H.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2002 v.99 no.16 pp. 10266-10271
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Nephila; silk; molecular conformation; nuclear magnetic resonance spectroscopy; Show all 5 Subjects
- Abstract:
- ... The design principles of spider dragline silk, nature's high-performance fiber, are still largely unknown, in particular for the noncrystalline glycine-rich domains, which form the bulk of the material. Here we apply two-dimensional solid-state NMR to determine the distribution of the backbone torsion angles (phi,psi) as well as the orientation of the polypeptide backbone toward the fiber at both ...
- DOI:
- 10.1073/pnas.152162299
- PubMed:
- 12149440
- PubMed Central:
- PMC124902
- http://dx.doi.org/10.1073/pnas.152162299
- Author:
- Tu, Z.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2001 v.98 no.4 pp. 1699-1704
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; genome; mutation; Anopheles gambiae; DNA conformation; transposons; gene dosage; Show all 7 Subjects
- DOI:
- 10.1073/pnas.98.4.1699
- PubMed:
- 11172014
- PubMed Central:
- PMC29320
- http://dx.doi.org/10.1073/pnas.98.4.1699
- Author:
- Vergunst, A.C.; Lier, M.C.M. van; Dulk-Ras, A. den; Grosse Stuve, T.A.; Ouwehand, A.; Hooykaas, P.J.J.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2005 v.102 no.3 pp. 832-837
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Arabidopsis thaliana; genetic transformation; Agrobacterium radiobacter; transfer DNA; bacterial diseases of plants; protein transport; bacterial proteins; signal peptide; DNA-binding proteins; site-directed mutagenesis; virulence; Show all 12 Subjects
- Abstract:
- ... Several human pathogens and the plant pathogen Agrobacterium tumefaciens use a type IV secretion system for translocation of effector proteins into host cells. How effector proteins are selected for transport is unknown, but a C-terminal transport signal is present in the proteins translocated by the A. tumefaciens VirB/D4 type IV secretion system. We characterized this signal in the virulence pro ...
- DOI:
- 10.1073/pnas.0406241102
- PubMed:
- 15644442
- PubMed Central:
- PMC545537
- http://dx.doi.org/10.1073/pnas.0406241102
- Author:
- Botuyan, M.V.; Koth, C.M.; Mer, G.; Chakrabartty, A.; Conaway, J.W.; Conaway, R.C.; Edwards, A.M.; Arrowsmith, C.H.; Chazin, W.J.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1999 v.96 no.16 pp. 9033-9038
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Saccharomyces cerevisiae; transcription factors; peptides; molecular conformation; dissociation; nuclear magnetic resonance spectroscopy; Show all 7 Subjects
- Abstract:
- ... Elongin is a heterotrimeric transcription elongation factor composed of subunits A, B, and C in mammals. Elongin A and C are F-box-containing and SKP1 homologue proteins, respectively, and are therefore of interest for their potential roles in cell cycle-dependent proteolysis. Mammalian elongin C interacts with both elongin A and elongin B, as well as with the von Hippel-Lindau tumor suppressor pr ...
- DOI:
- 10.1073/pnas.96.16.9033
- PubMed:
- 10430890
- PubMed Central:
- PMC17727
- http://dx.doi.org/10.1073/pnas.96.16.9033
- Author:
- Wilk, K.E.; Harrop, S.J.; Jankova, L.; Edler, D.; Keenan, G.; Sharples, F.; Hiller, R.G.; Curmi, P.M.G.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1999 v.96 no.16 pp. 8901-8906
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; X-ray diffraction; algae; light harvesting complex; crystals; Rhodomonas; molecular conformation; Show all 7 Subjects
- Abstract:
- ... Cryptophytes are unicellular photosynthetic algae that use a lumenally located light-harvesting system, which is distinct from the phycobilisome structure found in cyanobacteria and red algae. One of the key components of this system is water-soluble phycoerythrin (PE) 545 whose expression is enhanced by low light levels. The crystal structure of the heterodimeric alpha(1)alpha(2)betabeta PE 545 f ...
- DOI:
- 10.1073/pnas.96.16.8901
- http://dx.doi.org/10.1073/pnas.96.16.8901
- Author:
- Horst, R.; Damberger, F.; Luginbuhl, P.; Guntert, P.; Peng, G.; Nikonova, L.; Leal, W.S.; Wuthrich, K.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2001 v.98 no.25 pp. 14374-14379
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Bombyx mori; binding proteins; receptors; pheromones; molecular conformation; pH; nuclear magnetic resonance spectroscopy; binding sites; Show all 9 Subjects
- Abstract:
- ... Odorants are transmitted by small hydrophobic molecules that cross the aqueous sensillar lymph surrounding the dendrites of the olfactory neurons to stimulate the olfactory receptors. In insects, the transport of pheromones, which are a special class of odorants, is mediated by pheromone-binding proteins (PBPs), which occur at high concentrations in the sensillar lymph. The PBP from the silk moth ...
- DOI:
- 10.1073/pnas.251532998
- PubMed:
- 11724947
- PubMed Central:
- PMC64689
- http://dx.doi.org/10.1073/pnas.251532998
- Author:
- Sagermann, M.; Stevens, T.H.; Matthews, B.W.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2001 v.98 no.13 pp. 7134-7139
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; X-ray diffraction; Saccharomyces cerevisiae; adenosinetriphosphatase; vacuoles; tonoplast; crystals; molecular conformation; amino acid sequences; Show all 9 Subjects
- Abstract:
- ... In contrast to the F-type ATPases, which use a proton gradient to generate ATP, the V-type enzymes use ATP to actively transport protons into organelles and extracellular compartments. We describe here the structure of the H-subunit (also called Vma13p) of the yeast enzyme. This is the first structure of any component of a V-type ATPase. The H-subunit is not required for assembly but plays an esse ...
- DOI:
- 10.1073/pnas.131192798
- PubMed:
- 11416198
- PubMed Central:
- PMC34635
- http://dx.doi.org/10.1073/pnas.131192798
- Author:
- Bolter, B.; Soll, J.; Schulz, A.; Hinnah, S.; Wagner, R.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1998 v.95 no.26 pp. 15831-15836
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; proteins; Synechocystis; protein transport; electric current; electrophysiology; lipid bilayers; molecular conformation; immunocytochemistry; Show all 9 Subjects
- Abstract:
- ... During evolution, chloroplasts have relinquished the majority of their genes to the nucleus. The products of transferred genes are imported into the organelle with the help of an import machinery that is distributed across the inner and outer plastid membranes. The evolutionary origin of this machinery is puzzling because, in the putative predecessors, the cyanobacteria, the outer two membranes, t ...
- DOI:
- 10.1073/pnas.95.26.15831
- PubMed:
- 9861056
- PubMed Central:
- PMC28130
- http://dx.doi.org/10.1073/pnas.95.26.15831
- Author:
- Lambert, J.D.; Moran, N.A.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1998 v.95 no.8 pp. 4458-4462
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; bacteria; symbionts; Wolbachia pipientis; insect pests; ribosomal RNA; phylogeny; mutation; Show all 8 Subjects
- Abstract:
- ... In populations that are small and asexual, mutations with slight negative effects on fitness will drift to fixation more often than in large or sexual populations in which they will be eliminated by selection. If such mutations occur in substantial numbers, the combined effects of long-term asexuality and small population size may result in substantial accumulation of mildly deleterious substituti ...
- DOI:
- 10.1073/pnas.95.8.4458
- PubMed:
- 9539759
- PubMed Central:
- PMC22511
- http://dx.doi.org/10.1073/pnas.95.8.4458
- Author:
- Friederich, M.W.; Vacano, E.; Hagerman, P.J.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1998 v.95 no.7 pp. 3572-3577
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Saccharomyces cerevisiae; transfer RNA; phenylalanine; molecular conformation; magnesium; electrophoresis; electrical properties; Show all 8 Subjects
- Abstract:
- ... The study of RNA structure using x-ray crystallography or NMR has yielded a wealth of detailed structural information; however, such approaches do not generally yield quantitative information regarding long-range flexibility in solution. To address this issue, we describe a solution-based method that is capable of characterizing the global flexibilities of nonhelix elements in RNA, provided that s ...
- DOI:
- 10.1073/pnas.95.7.3572
- PubMed:
- 9520407
- PubMed Central:
- PMC19877
- http://dx.doi.org/10.1073/pnas.95.7.3572
30. A novel type of RNA editing occurs in the mitochondrial tRNAs of the centipede Lithobius forficatus
- Author:
- Lavrov, D.V.; Brown, W.M.; Boore, J.L.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2000 v.97 no.25 pp. 13738-13742
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; RNA editing; mitochondrial DNA; nucleotide sequences; transfer RNA; genes; complementary DNA; molecular conformation; genomics; Lithobius forficatus; Show all 10 Subjects
- DOI:
- 10.1073/pnas.250402997
- PubMed:
- 11095730
- PubMed Central:
- PMC17645
- http://dx.doi.org/10.1073/pnas.250402997
- Author:
- Heddad, M.; Adamska, I.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2000 v.97 no.7 pp. 3741-3746
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Arabidopsis thaliana; nucleotide sequences; amino acid sequences; molecular conformation; gene expression; light intensity; messenger RNA; cytochemistry; thylakoids; Show all 10 Subjects
- Abstract:
- ... The chlorophyll a/b, chlorophyll a/c, and chlorophyll a/a light-harvesting proteins are part of an extended gene family that also includes the transiently expressed stress proteins, the Elips (early light-induced proteins). Four Elip homologue proteins, encoded by single-copy nuclear genes, have been identified in the Arabidopsis thaliana database. These proteins were divided into two groups accor ...
- DOI:
- 10.1073/pnas.97.7.3741
- PubMed:
- 10725357
- PubMed Central:
- PMC16310
- http://dx.doi.org/10.1073/pnas.97.7.3741
- Author:
- Bharathan, G.; Janssen, B.J.; Kellogg, E.A.; Sinha, N.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1997 v.94 no.25 pp. 13749-13753
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; transcription factors; animals; phylogeny; genes; DNA-binding domains; Angiospermae; molecular conformation; fungi; Show all 9 Subjects
- Abstract:
- ... Homeodomain proteins are transcription factors that play a critical role in early development in eukaryotes. These proteins previously have been classified into numerous subgroups whose phylogenetic relationships are unclear. Our phylogenetic analysis of representative eukaryotic sequences suggests that there are two major groups of homeodomain proteins, each containing sequences from angiosperms, ...
- DOI:
- 10.1073/pnas.94.25.13749
- PubMed:
- 9391098
- PubMed Central:
- PMC28378
- http://dx.doi.org/10.1073/pnas.94.25.13749
- Author:
- Howe, K.J.; Ares, M. Jr.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1997 v.94 no.23 pp. 12467-12472
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; messenger RNA; alternative splicing; mutation; Saccharomyces cerevisiae; introns; molecular conformation; Show all 7 Subjects
- Abstract:
- ... Skipping of internal exons during removal of introns from pre-mRNA must be avoided for proper expression of most eukaryotic genes. Despite significant understanding of the mechanics of intron removal, mechanisms that ensure inclusion of internal exons in multi-intron pre-mRNAs remain mysterious. Using a natural two-intron yeast gene, we have identified distinct RNA-RNA complementarities within eac ...
- DOI:
- 10.1073/pnas.94.23.12467
- PubMed:
- 9356473
- PubMed Central:
- PMC25003
- http://dx.doi.org/10.1073/pnas.94.23.12467
34. Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments
- Author:
- King, C.Y.; Tittmann, P.; Gross, H.; Gebert, R.; Aebi, M.; Wuthrich, K.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1997 v.94 no.13 pp. 6618-6622
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Saccharomyces cerevisiae; prions; molecular conformation; cell structures; amyloid; Show all 6 Subjects
- Abstract:
- ... The yeast non-Mendelian genetic factor [PSI], which enhances the efficiency of tRNA-mediated non-sense suppression in Saccharomyces cerevisiae, is thought to be an abnormal cellular isoform of the Sup35 protein. Genetic studies have established that the N-terminal part of the Sup35 protein is sufficient for the genesis as well as the maintenance of [PSI]. Here we demonstrate that the N-terminal po ...
- DOI:
- 10.1073/pnas.94.13.6618
- PubMed:
- 9192614
- PubMed Central:
- PMC21207
- http://dx.doi.org/10.1073/pnas.94.13.6618
- Author:
- Gursky, O.; Atkinson, D.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1996 v.93 no.7 pp. 2991-2995
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; enthalpy; humans; apolipoproteins; protein tertiary structure; differential scanning calorimetry; molecular conformation; spectroscopy; Show all 8 Subjects
- Abstract:
- ... Apolipoprotein A-1 (apoA-1) in complex with high-density lipoprotein is critically involved in the transport and metabolism of cholesterol and in the pathogenesis of atherosclerosis. We reexamined the thermal unfolding of lipid-free apoA-1 in low-salt solution at pH approximately 7, by using differential scanning calorimetry and circular dichroism. At protein concentrations < 5 mg/ml, thermal unfo ...
- DOI:
- 10.1073/pnas.93.7.2991
- PubMed:
- 8610156
- PubMed Central:
- PMC39748
- http://dx.doi.org/10.1073/pnas.93.7.2991
- Author:
- Marle, G. van.; Dobbe, J.C.; Gultyaev, A.P.; Luytjes, W.; Spaan, W.J.M.; Snijder, E.J.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1999 v.96 no.21 pp. 12056-12061
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; messenger RNA; complementary DNA; Equine arteritis virus; clones; transcription (genetics); nucleotide sequences; site-directed mutagenesis; molecular conformation; Show all 9 Subjects
- Abstract:
- ... To generate an extensive set of subgenomic (sg) mRNAs, nidoviruses (arteriviruses and coronaviruses) use a mechanism of discontinuous transcription. During this process, mRNAs are generated that represent the genomic 5' sequence, the so-called leader RNA, fused at specific positions to different 3' regions of the genome. The fusion of the leader to the mRNA bodies occurs at a short, conserved sequ ...
- DOI:
- 10.1073/pnas.96.21.12056
- PubMed:
- 10518575
- PubMed Central:
- PMC18411
- http://dx.doi.org/10.1073/pnas.96.21.12056
- Author:
- Gibbs, M.J.; Weiller, G.F.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1999 v.96 no.14 pp. 8022-8027
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; plant viruses; Caliciviridae; replication origin; phylogeny; amino acid sequences; viral proteins; Porcine circovirus; molecular conformation; genetic recombination; Show all 10 Subjects
- Abstract:
- ... There are several similarities between the small, circular, single-stranded-DNA genomes of circoviruses that infect vertebrates and the nanoviruses that infect plants. We analyzed circovirus and nanovirus replication initiator protein (Rep) sequences and confirmed that an N-terminal region in circovirus Reps is similar to an equivalent region in nanovirus Reps. However, we found that the remaining ...
- DOI:
- 10.1073/pnas.96.14.8022
- PubMed:
- 10393941
- PubMed Central:
- PMC22181
- http://dx.doi.org/10.1073/pnas.96.14.8022
- Author:
- Knubovets, T.; Osterhout, J.J.; Connolly, P.J.; Klibanov, A.M.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1999 v.96 no.4 pp. 1262-1267
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; lysozyme; nuclear magnetic resonance spectroscopy; heat stability; protein tertiary structure; glycerol; spectral analysis; molecular conformation; egg albumen; Show all 9 Subjects
- Abstract:
- ... Hen egg-white lysozyme dissolved in glycerol containing 1% water was studied by using CD and amide proton exchange monitored by two-dimensional 1H NMR. The far- and near-UV CD spectra of the protein showed that the secondary and tertiary structures of lysozyme in glycerol were similar to those in water. Thermal melting of lysozyme in glycerol followed by CD spectral changes indicated unfolding of ...
- DOI:
- 10.1073/pnas.96.4.1262
- PubMed:
- 9990012
- PubMed Central:
- PMC15451
- http://dx.doi.org/10.1073/pnas.96.4.1262
- Author:
- Breckenridge, D.G.; Watanabe, Y.; Greenwood, S.J.; Gray, M.W.; Schnare, M.N.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1999 v.96 no.3 pp. 852-856
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; proteins; messenger RNA; alternative splicing; structural genes; complementary DNA; small nuclear RNA; molecular conformation; introns; Euglena gracilis; Show all 10 Subjects
- Abstract:
- ... In the flagellated protozoon Euglena gracilis, characterized nuclear genes harbor atypical introns that usually are flanked by short repeats, adopt complex secondary structures in pre-mRNA, and do not obey the GT-AG rule of conventional cis-spliced introns. In the nuclear fibrillarin gene of E. gracilis, we have identified three spliceosomal-type introns that have GT-AG consensus borders. Furtherm ...
- DOI:
- 10.1073/pnas.96.3.852
- PubMed:
- 9927657
- PubMed Central:
- PMC15314
- http://dx.doi.org/10.1073/pnas.96.3.852
- Author:
- Kachroo, P.; Leong, S.A.; Chattoo, B.B.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1995 v.92 no.24 pp. 11125-11129
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Southern blotting; messenger RNA; Magnaporthe grisea; DNA conformation; Northern blotting; transposons; Show all 7 Subjects
- Abstract:
- ... A short interspersed nuclear element, Mg-SINE, was isolated and characterized from the genome of the rice blast fungus, Magnaporthe grisea. Mg-SINE was isolated as an insertion element within Pot2, an inverted-repeat transposon from M. grisea and shows typical features of a mammalian SINE. Mg-SINE is present as a 0.47-kb interspersed sequence at approximately 100 copies per haploid genome in both ...
- DOI:
- 10.1073/pnas.92.24.11125
- PubMed:
- 7479950
- PubMed Central:
- PMC40584
- http://dx.doi.org/10.1073/pnas.92.24.11125
- Author:
- Bourne, Y.; Arvai, A.S.; Bernstein, S.L.; Watson, M.H.; Reed, S.I.; Endicott, J.E.; Nobel, M.E.; Johnson, L.N.; Tainer, J.A.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1995 v.92 no.22 pp. 10232-10236
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; X-ray diffraction; Saccharomycetales; proteins; molecular conformation; Schizosaccharomyces pombe; Show all 6 Subjects
- Abstract:
- ... The Schizosaccharomyces pombe cell cycle-regulatory protein suc1, named as the suppressor of cdc2 temperature-sensitive mutations, is essential for cell cycle progression. To understand suc1 structure-function relationships and to help resolve conflicting interpretations of suc1 function based on genetic studies of suc1 and its functional homologs in both lower and higher eukaryotes, we have deter ...
- DOI:
- 10.1073/pnas.92.22.10232
- PubMed:
- 7479758
- PubMed Central:
- PMC40770
- http://dx.doi.org/10.1073/pnas.92.22.10232
- Author:
- Dubchak, I.; Muchnik, I.; Holbrook, S.R.; Kim, S.H.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1995 v.92 no.19 pp. 8700-8704
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; proteins; molecular conformation; amino acid sequences; prediction; computer analysis; hydrophobicity; solvents; neural networks; Show all 9 Subjects
- Abstract:
- ... We present a method for predicting protein folding class based on global protein chain description and a voting process. Selection of the best descriptors was achieved by a computer-simulated neural network trained on a data base consisting of 83 folding classes. Protein-chain descriptors include overall composition, transition, and distribution of amino acid attributes, such as relative hydrophob ...
- DOI:
- 10.1073/pnas.92.19.8700
- PubMed:
- 7568000
- PubMed Central:
- PMC41034
- http://dx.doi.org/10.1073/pnas.92.19.8700
- Author:
- Rackovsky, S.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1995 v.92 no.15 pp. 6861-6863
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; proteins; amino acid sequences; molecular conformation; protein folding; Show all 5 Subjects
- Abstract:
- ... The existence of a code relating the set of possible sequences at a given position in a protein backbone to the local structure at that location is investigated. It is shown that only 73% of 4-C alpha structure fragments in a sample of 114 protein structures exhibit a preference for a particular set of sequences. The remaining structures can accommodate essentially any sequence. The structures tha ...
- DOI:
- 10.1073/pnas.92.15.6861
- PubMed:
- 7624332
- PubMed Central:
- PMC41429
- http://dx.doi.org/10.1073/pnas.92.15.6861
- Author:
- Basham, B.; Schroth, G.P.; Ho, P.S.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1995 v.92 no.14 pp. 6464-6468
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; DNA; nucleotide sequences; prediction; thermodynamics; energy; DNA conformation; spectroscopy; Show all 8 Subjects
- Abstract:
- ... The ability to predict macromolecular conformations from sequence and thermodynamic principles has long been coveted but generally has not been achieved. We show that differences in the hydration of DNA surfaces can be used to distinguish between sequences that form A- and B-DNA. From this, a "triplet code" of A-DNA propensities was derived as energetic rules for predicting A-DNA formation. This c ...
- DOI:
- 10.1073/pnas.92.14.6464
- PubMed:
- 7604014
- PubMed Central:
- PMC41538
- http://dx.doi.org/10.1073/pnas.92.14.6464
- Author:
- France, L.L.; Piatti, P.G.; Newman, J.F.E.; Toth, I.; Gibbons, W.A.; Brown, F.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1994 v.91 no.18 pp. 8442-8446
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Aphthovirus; viral proteins; molecular conformation; antigenic variation; synthetic peptides; epitopes; spectroscopy; viral antigens; Show all 9 Subjects
- Abstract:
- ... Seven antigenic variants obtained from a single field isolate of foot-and-mouth disease virus, serotype A12, differ only at residues 148 and 153 in the immunodominant loop of viral protein VP1. Synthetic peptides corresponding to the region 141-160 are highly immunogenic. UV circular dichroism shows that (i) in aqueous solution the peptides are nearly identical, but in 100% trifluoroethanol they d ...
- DOI:
- 10.1073/pnas.91.18.8442
- http://dx.doi.org/10.1073/pnas.91.18.8442
- Author:
- Hehl, A.; Vassella, E.; Braun, R.; Roditi, I.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1994 v.91 no.1 pp. 370-374
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Trypanosoma brucei; messenger RNA; molecular conformation; microbial proteins; developmental stages; gene expression; Show all 7 Subjects
- Abstract:
- ... African trypanosomes that cycle between mammalian hosts and the tsetse fly vector must be poised to survive in different environments. The control of stage-specific gene expression is undoubtedly one of the keys to successful adaptation, but no regulatory elements have been defined to date. Procyclins (also known as procyclic acidic repetitive proteins) are specifically expressed on the surface of ...
- DOI:
- 10.1073/pnas.91.1.370
- PubMed:
- 8278396
- PubMed Central:
- PMC42949
- http://dx.doi.org/10.1073/pnas.91.1.370
- Author:
- Muramoto, T.; Scott, M.; Cohen, F.E.; Prusiner, S.B.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1996 v.93 no.26 pp. 15457-15462
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; neurons; animal proteins; recombinant proteins; PrPSc proteins; transgenic animals; mice; solubility; detergents; molecular conformation; Show all 10 Subjects
- Abstract:
- ... The N terminus of the scrapie isoform of prion protein (PrP(Sc)) can be truncated without loss of scrapie infectivity and, correspondingly, the truncation of the N terminus of the cellular isoform, PrP(C), still permits conversion into PrP(Sc). To assess whether additional segments of the PrP molecule can be deleted, we previously removed regions of putative secondary structure in PrP(C); in the p ...
- DOI:
- 10.1073/pnas.93.26.15457
- PubMed:
- 8986833
- PubMed Central:
- PMC26426
- http://dx.doi.org/10.1073/pnas.93.26.15457
- Author:
- Giege, P.; Brennicke, A.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1999 v.96 no.26 pp. 15324-15329
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Arabidopsis thaliana; messenger RNA; complementary DNA; open reading frames; mitochondrial DNA; codons; mitochondria; hydrophobicity; RNA editing; molecular conformation; plant proteins; Show all 12 Subjects
- Abstract:
- ... On the basis of the sequence of the mitochondrial genome in the flowering plant Arabidopsis thaliana, RNA editing events were systematically investigated in the respective RNA population. A total of 456 C to U, but no U to C, conversions were identified exclusively in mRNAs, 441 in ORFs, 8 in introns, and 7 in leader and trailer sequences. No RNA editing was seen in any of the rRNAs or in several ...
- DOI:
- 10.1073/pnas.96.26.15324
- PubMed:
- 10611383
- PubMed Central:
- PMC24818
- http://dx.doi.org/10.1073/pnas.96.26.15324
- Author:
- Ansari, A.Z.; Reece, R.J.; Ptashne, M.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1998 v.95 no.23 pp. 13543-13548
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Saccharomyces cerevisiae; transcription factors; DNA-binding proteins; cysteine; proline; mutants; molecular conformation; gene expression; reporter genes; beta-galactosidase; transcription (genetics); binding sites; site-directed mutagenesis; Show all 14 Subjects
- Abstract:
- ... A C-terminal segment of the yeast activator Gal4 manifests two functions: When tethered to DNA, it elicits gene activation, and it binds the inhibitor Gal80. Here we examine the effects on these two functions of cysteine and proline substitutions. We find that, although certain cysteine substitutions diminish interaction with Gal80, those substitutions have little effect on the activating function ...
- DOI:
- 10.1073/pnas.95.23.13543
- PubMed:
- 9811836
- PubMed Central:
- PMC24855
- http://dx.doi.org/10.1073/pnas.95.23.13543
- Author:
- Laten, H.M.; Majumdar, A.; Gaucher, E.A.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1998 v.95 no.12 pp. 6897-6902
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; RNA-directed DNA polymerase; retrotransposons; Glycine max; Retroviridae; transmembrane proteins; open reading frames; amino acid sequences; molecular conformation; Show all 9 Subjects
- Abstract:
- ... The soybean genome hosts a family of several hundred, relatively homogeneous copies of a large, copia/Ty1-like retroelement designated SIRE-1. A copy of this element has been recovered from a Glycine max genomic library. DNA sequence analysis of two SIRE-1 subclones revealed that SIRE-1 contains a long, uninterrupted, ORF between the 3' end of the pol ORF and the 3' long terminal repeat (LTR), a r ...
- DOI:
- 10.1073/pnas.95.12.6897
- PubMed:
- 9618510
- PubMed Central:
- PMC22677
- http://dx.doi.org/10.1073/pnas.95.12.6897
51. Phylogeny of hard- and soft-tick taxa (Acari: Ixodida) based on mitochondrial 16S rDNA sequences
- Author:
- Black, W.C. IV; Piesman, J.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1994 v.91 no.21 pp. 10034-10038
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Ixodidae; Argasidae; ribosomal DNA; ribosomal RNA; structural genes; nucleotide sequences; mitochondrial DNA; phylogeny; molecular conformation; Show all 10 Subjects
- Abstract:
- ... Ticks are parasitiform mites that are obligate hematophagous ectoparasites of amphibians, reptiles, birds, and mammals. A phylogeny for tick families, subfamilies, and genera has been described based on morphological characters, life histories, and host associations. To test the existing phylogeny, we sequenced approximately 460 bp from the 3' end of the mitochondrial 16S rRNA gene (rDNA) in 36 ha ...
- DOI:
- 10.1073/pnas.91.21.10034
- PubMed:
- 7937832
- PubMed Central:
- PMC44952
- http://dx.doi.org/10.1073/pnas.91.21.10034
- Author:
- Singh, M.; Boutanaev, A.; Zucchi, P.; Bogorad, L.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 2001 v.98 no.5 pp. 2289-2294
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; ribulose-bisphosphate carboxylase; messenger RNA; recombinant DNA; chloroplast DNA; mutation; reporter genes; ribonucleases; Chlamydomonas reinhardtii; degradation; genomics; molecular conformation; promoter regions; beta-glucuronidase; light; half life; Show all 16 Subjects
- Abstract:
- ... The chloroplast gene rbcL encodes the large subunit of the CO2-fixing enzyme ribulose-bisphosphate carboxylase. In previous work a target for photo-accelerated degradation of Chlamydomonas reinhardtii rbcL transcripts in vivo was found to lie within the first 63 nucleotides, and a sequence element required for increasing the longevity of transcripts of rbcL-reporter genes was found to occur betwee ...
- DOI:
- 10.1073/pnas.041609798
- PubMed:
- 11226232
- PubMed Central:
- PMC30131
- http://dx.doi.org/10.1073/pnas.041609798
- Author:
- Navarro, B.; Flores, R.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1997 v.94 no.21 pp. 11262-11267
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Chrysanthemum chlorotic mottle viroid; chemical reactions; physicochemical properties; transcription (genetics); pathogenicity; Chrysanthemum morifolium; nucleotide sequences; lithium chloride; RNA; molecular conformation; Show all 11 Subjects
- Abstract:
- ... The causal agent of chrysanthemum chlorotic mottle (CChM) disease has been identified, cloned, and sequenced. It is a viroid RNA (CChMVd) of 398-399 nucleotides. In vitro transcripts with the complete CChMVd sequence were infectious and induced the typical symptoms of the CChM disease. CChMVd can form hammerhead structures in both polarity strands. Plus and minus monomeric CChMVd RNAs self-cleaved ...
- DOI:
- 10.1073/pnas.94.21.11262
- PubMed:
- 9326597
- PubMed Central:
- PMC23434
- http://dx.doi.org/10.1073/pnas.94.21.11262
- Author:
- Hiesel, R.; Haeseler, A. von.; Brennicke, A.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1994 v.91 no.2 pp. 634-638
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Polypodiopsida; structural genes; mitochondrial DNA; complementary DNA; phylogeny; Chlorophyta; cytochrome-c oxidase; Triticum aestivum; ferns and fern allies; molecular conformation; Gymnospermae; Bryopsida; introns; Oenothera; Show all 15 Subjects
- Abstract:
- ... To evaluate the potential of mitochondrial nucleic acid sequences as a phylogenetic tool, we have analyzed cytochrome oxidase subunit III (coxIII) coding sequences in representatives of the major groups of land plants. The phylogenetic tree derived from these mitochondrial sequences confirms the monophyletic origin of land plant mitochondria with the general order and descent of land plants deduce ...
- DOI:
- 10.1073/pnas.91.2.634
- PubMed:
- 7507251
- PubMed Central:
- PMC43003
- http://dx.doi.org/10.1073/pnas.91.2.634
- Author:
- Jin, L.; Cohen, F.E.; Wells, J.A.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1994 v.91 no.1 pp. 113-117
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; humans; somatotropin; molecular conformation; prediction; epitopes; monoclonal antibodies; simulation models; algorithms; computer analysis; mutants; molecular models; binding sites; site-directed mutagenesis; Show all 14 Subjects
- Abstract:
- ... Structural constraints derived from different antibody epitopes on human growth hormone (hGH) were used to screen three-dimensional models of hGH that were generated by computer algorithms. Previously, alanine-scanning mutagenesis defined the residues that modulate binding to 21 different monoclonal antibodies to hGH. These functional epitopes were composed of 4-14 side chains whose alpha-carbons ...
- DOI:
- 10.1073/pnas.91.1.113
- PubMed:
- 7506411
- PubMed Central:
- PMC42896
- http://dx.doi.org/10.1073/pnas.91.1.113
- Author:
- Schachtman, D.P.; Kumar, R.; Schroeder, J.I.; Marsh, E.L.
- Source:
- Proceedings of the National Academy of Sciences of the United States of America 1997 v.94 no.20 pp. 11079-11084
- ISSN:
- 0027-8424
- Subject:
- protein secondary structure, etc ; Triticum aestivum; complementary DNA; plant proteins; nucleotide sequences; amino acid sequences; molecular conformation; ion transport; sodium; rubidium; roots; leaves; mutants; Saccharomyces cerevisiae; plasma membrane; inorganic ions; calcium; genetic complementation; Show all 18 Subjects
- Abstract:
- ... The transport of cations across membranes in higher plants plays an essential role in many physiological processes including mineral nutrition, cell expansion, and the transduction of environmental signals. In higher plants the coordinated expression of transport mechanisms is essential for specialized cellular processes and for adaptation to variable environmental conditions. To understand the mo ...
- DOI:
- 10.1073/pnas.94.20.11079
- PubMed:
- 9380762
- PubMed Central:
- PMC23614
- http://dx.doi.org/10.1073/pnas.94.20.11079