Pro----Ala-35 Rhodobacter capsulatus cytochrome c2 shows dynamic not structural differences. A 1H and 15N NMR study.
Comparative analysis of nuclear Overhauser effects show that the time average conformation of the wild-type and mutant Pro----Ala-35 Rhodobacter capsulatus cytochrome c2 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 NpiH of His-17 increase by approximately 10(2) in P35A suggesting that their respective hydrogen bonds are destabilized in this protein. However, 3JchiNH 1H and 15N 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.
Gooley
P R
PR
Dept. of Pharmaceutical Sciences, College of Pharmacy, University of Arizona, Tucson 85721.
MacKenzie
N E
NE
D000409:Alanine; D003574:Cytochrome c Group / Q000032:analysis* / Q000235:genetics / Q000502:physiology; D045362:Cytochromes c2; D004795:Enzyme Stability; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D009154:Mutation; D011392:Proline; D011487:Protein Conformation; D012244:Rhodospirillaceae / Q000201:enzymology* / Q000235:genetics
D003574:Cytochrome c Group; D045362:Cytochromes c2; D011392:Proline; D000409:Alanine