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Pro → Ala‐35 Rhodobacter capsulatus cytochrome c 2 shows dynamic not structural differences
Author(s) -
Gooley Paul R.,
MacKenzie Neil E.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80109-v
Subject(s) - rhodobacter , cytochrome , chemistry , biochemistry , mutant , gene , enzyme
Comparative analysis of nuclear Overhauser effects show that the time average conformation of the wild‐type and mutant Pro → Ala‐35 Rhodobacter capsulatus cytochrome c 2 are indistinguishable. The ring resonances of Phe‐51 and Tyr‐53 show that their ring flip rates increase in P35A. NH proton exchange studies show that the exchange rates of the NH of Gly‐34 and the N π H of His‐17 increase by ≈ 10 2 in P35A suggesting that their respective hydrogen bonds are destabilized in this protein. However, 3 αNH . 1 H and 15 N chemical shift data argue that these bonds are intact. These data are compatible if the replacement of a Pro with an Ala residue forms a cavity or increases local flexibility thus reducing steric hinderance and increasing solvent accessibility.