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You searched for: Journal name Biochemistry Remove constraint Journal name: Biochemistry Subject term chemical interactions Remove constraint Subject term: chemical interactions Subject term models Remove constraint Subject term: models
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1. An Initial Event in the Insect Innate Immune Response: Structural and Biological Studies of Interactions between β-1,3-Glucan and the N-Terminal Domain of β-1,3-Glucan Recognition Protein

Author:
Dai Huaien; Hiromasa Yasuaki; Takahashi Daisuke; VanderVelde David; Fabrick Jeffrey A.; Kanost Michael R.; Krishnamoorthi Ramaswamy
Source:
Biochemistry 2013 v.52 no.1 pp. 161-170
ISSN:
1520-4995
Subject:
Plodia interpunctella; X-ray diffraction; antimicrobial peptides; bacteria; beta-glucans; calorimetry; chemical interactions; crystal structure; dissociation; electrostatic interactions; fungi; glucose; hemolymph; innate immunity; insects; melanin; melanization; models; monophenol monooxygenase; mutants; nuclear magnetic resonance spectroscopy; pathogens; prophenoloxidase; serine proteinases; structure-activity relationships; ultracentrifugation
Abstract:
... In response to invading microorganisms, insect β-1,3-glucan recognition protein (βGRP), a soluble receptor in the hemolymph, binds to the surfaces of bacteria and fungi and activates serine protease cascades that promote destruction of pathogens by means of melanization or expression of antimicrobial peptides. Here we report on the nuclear magnetic resonance (NMR) solution structure of the N-termi ...
DOI:
10.1021/bi301440p
PubMed:
23237493
PubMed Central:
PMC3542770

2. Delicate Balance between Functionally Required Flexibility and Aggregation Risk in a β-Rich Protein

Author:
Ferrolino Mylene C.; Zhuravleva Anastasia; Budyak Ivan L.; Krishnan Beena; Gierasch Lila M.
Source:
Biochemistry 2013 v.52 no.49 pp. 8843-8854
ISSN:
1520-4995
Subject:
amino acid sequences; chemical interactions; hydrophobicity; models; proteins; risk
Abstract:
... Susceptibility to aggregation is general to proteins because of the potential for intermolecular interactions between hydrophobic stretches in their amino acid sequences. Protein aggregation has been implicated in several catastrophic diseases, yet we still lack in-depth understanding about how proteins are channeled to this state. Using a predominantly β-sheet protein whose folding has been explo ...
DOI:
10.1021/bi4013462
PubMed:
24236614
PubMed Central:
PMC3946317

3. Dimerization and Long-Range Repulsion Established by Both Termini of the Microtubule-Associated Protein Tau

Author:
Zachary J. Donhauser; Jared T. Saunders; Dennis S. D’Urso; Teresa A. Garrett
Source:
Biochemistry 2017 v.56 no.44 pp. 5900-5909
ISSN:
1520-4995
Subject:
atomic force microscopy; axons; chemical interactions; depolymerization; dimerization; electrolytes; electrostatic interactions; humans; ionic strength; mica; microtubules; models; mutants; polymerization; proteins; silicon nitride
Abstract:
... Tau is a microtubule-associated protein found in neuronal axons that has several well-known functions, such as promoting microtubule polymerization, stabilizing microtubules against depolymerization, and spatially organizing microtubules in axons. Two contrasting models have been previously described to explain tau’s ability to organize the spacing between microtubules: complementary dimerization ...
DOI:
10.1021/acs.biochem.7b00653
PubMed:
29039655
PubMed Central:
PMC6613632

4. Effect of the Flexible Regions of the Oncoprotein Mouse Double Minute X on Inhibitor Binding Affinity

Author:
Lingyun Qin; Huili Liu; Rong Chen; Jingjing Zhou; Xiyao Cheng; Yao Chen; Yongqi Huang; Zhengding Su
Source:
Biochemistry 2017 v.56 no.44 pp. 5943-5954
ISSN:
1520-4995
Subject:
amino acid sequences; binding capacity; chemical interactions; drugs; engineering; ligands; mice; models; molecular dynamics; mutants; oncogene proteins; pharmacology; prediction; protein conformation; protein engineering; screening
Abstract:
... The oncoprotein MdmX (mouse double minute X) is highly homologous to Mdm2 (mouse double minute 2) in terms of their amino acid sequences and three-dimensional conformations, but Mdm2 inhibitors exhibit very weak affinity for MdmX, providing an excellent model for exploring how protein conformation distinguishes and alters inhibitor binding. The intrinsic conformation flexibility of proteins plays ...
DOI:
10.1021/acs.biochem.7b00903

5. Noncoupled Fluorescent Assay for Direct Real-Time Monitoring of Nicotinamide N-Methyltransferase Activity

Author:
Neelakantan Harshini; Vance Virginia; Wang Hua-Yu Leo; McHardy Stanton F.; Watowich Stanley J.
Source:
Biochemistry 2017 v.56 no.6 pp. 824-832
ISSN:
1520-4995
Subject:
Parkinson disease; apoproteins; cardiovascular diseases; chemical interactions; chronic diseases; data collection; fluorescence; fluorescence emission spectroscopy; kidney diseases; metabolic diseases; models; monitoring; neoplasms; nicotinamide N-methyltransferase; osteoarthritis; screening
Abstract:
... Nicotinamide N-methyltransferase (NNMT) is an important biotransforming enzyme that catalyzes the transfer of a labile methyl group from the ubiquitous cofactor S-5′-adenosyl-l-methionine (SAM) to endogenous and exogenous small molecules to form methylated end products. NNMT has been implicated in a number of chronic disease conditions, including metabolic disorders, cardiovascular disease, cancer ...
DOI:
10.1021/acs.biochem.6b01215

6. Pif97, a von Willebrand and Peritrophin Biomineralization Protein, Organizes Mineral Nanoparticles and Creates Intracrystalline Nanochambers

Author:
Chang Eric P.; Evans John Spencer
Source:
Biochemistry 2015 v.54 no.34 pp. 5348-5355
ISSN:
1520-4995
Subject:
Pinctada fucata; aragonite; biomineralization; calcite; calcium carbonate; chemical interactions; coatings; crystals; models; nacre; nanoparticles; oysters; porosity; proteome
Abstract:
... The formation of the mollusk nacre layer involves the assembly and organization of mineral nanoparticles into fracture-toughened mesoscale-sized aragonite tablets that possess intracrystalline nanoporosities. At least one nacre protein family, known as the framework proteome, is strategically located as part of a macromolecular coating around each nacre tablet and is believed to participate in tab ...
DOI:
10.1021/acs.biochem.5b00842

7. Structure of an As(III) S-Adenosylmethionine Methyltransferase: Insights into the Mechanism of Arsenic Biotransformation

Author:
Ajees A. Abdul; Marapakala Kavitha; Packianathan Charles; Sankaran Banumathi; Rosen Barry P.
Source:
Biochemistry 2012 v.51 no.27 pp. 5476-5485
ISSN:
1520-4995
Subject:
S-adenosylmethionine; X-ray diffraction; algae; arsenic; binding sites; biotransformation; catalytic activity; chemical interactions; enzyme substrates; humans; methylation; methyltransferases; microorganisms; models
Abstract:
... Enzymatic methylation of arsenic is a detoxification process in microorganisms but in humans may activate the metalloid to more carcinogenic species. We describe the first structure of an As(III) S-adenosylmethionine methyltransferase by X-ray crystallography that reveals a novel As(III) binding domain. The structure of the methyltransferase from the thermophilic eukaryotic alga Cyanidioschyzon me ...
DOI:
10.1021/bi3004632
PubMed:
22712827
PubMed Central:
PMC3447999

8. We FRET so You Don’t Have To: New Models of the Lipoprotein Lipase Dimer

Author:
Cassandra K. Hayne; Hayretin Yumerefendi; Lin Cao; Jacob W. Gauer; Michael J. Lafferty; Brian Kuhlman; Dorothy A. Erie; Saskia B. Neher
Source:
Biochemistry 2018 v.57 no.2 pp. 241-254
ISSN:
1520-4995
Subject:
blood; chemical interactions; crystallography; dimerization; energy transfer; fluorescent dyes; image analysis; lipoprotein lipase; lipoproteins; models; mutation; nuclear magnetic resonance spectroscopy; patients; therapeutics; triacylglycerol lipase
Abstract:
... Lipoprotein lipase (LPL) is a dimeric enzyme that is responsible for clearing triglyceride-rich lipoproteins from the blood. Although LPL plays a key role in cardiovascular health, an experimentally derived three-dimensional structure has not been determined. Such a structure would aid in understanding mutations in LPL that cause familial LPL deficiency in patients and help in the development of t ...
DOI:
10.1021/acs.biochem.7b01009
PubMed:
29303250
PubMed Central:
PMC5860654