Jump to Main Content
- Strobl, S.; Muhlhahn, P.; Bernstein, R.; Wiltscheck, R.; Maskos, K.; Wunderlich, M.; Huber, R.; Glockshuber, R.; Holak, T.A.
- Biochemistry 1995 v.34 no.26 pp. 8281-8293
- Eleusine coracana subsp. coracana; alpha-amylase; amino acids; binding sites; disulfide bonds; nuclear magnetic resonance spectroscopy; proteinase inhibitors; seeds; topology; trypsin
- ... The three-dimensional structure of the bifunctional alpha-amylase/trypsin inhibitor (RBI) from seeds of ragi (Eleusine coracana Gaertneri) has been determined in solution using multidimensional 1H and 15N NMR spectroscopy. The inhibitor consists of 122 amino acids, with 5 disulfide bridges, and belongs to the plant alpha-amylase/trypsin inhibitor family for which no three-dimensional structures ha ...
- Sebban, P.; Maroti, P.; Schiffer, M.; Hanson, D.K.
- Biochemistry 1995 v.34 no.26 pp. 8390-8397
- Rhodobacter capsulatus; absorbance; bacteria; binding sites; energy; mutants; mutation; pH; phenotype; photosynthetic reaction centers; protons; spectroscopy
- ... Two point mutants from the purple bacterium Rhodobacter capsulatus, both modified in the M protein of the photosynthetic reaction center, have been studied by flash-induced absorbance spectroscopy. These strains carry either the M231Arg leads to Leu or M43Asn leads to Asp mutations, which are located 9 and 15 angstroms, respectively, from the terminal electron acceptor QB. In the wild-type Rb. sph ...