Correlation of folding kinetics with the number and isomerization states of prolines in three homologous proteins of the RNase family.
Several studies attribute the slower phases in protein folding to prolyl isomerizations, and several others do not. A correlation exists between the number of prolines in a protein and the complexity of the mechanism with which it folds. In this study, we have demonstrated a direct correlation between the number of cis-prolyl bonds in a native protein and the complexity with which it folds via slower phases by studying the folding of three structurally homologous proteins of the ribonuclease family, namely RNase A, onconase and angiogenin, which differ in the number and isomerization states of their proline residues.
Pradeep
Lovy
L
Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301, USA.
Shin
Hang-Cheol
HC
Scheraga
Harold A
HA
D000818:Animals; D001001:Anura; D002417:Cattle; D007700:Kinetics; D011392:Proline / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012259:Ribonuclease, Pancreatic / Q000737:chemistry* / Q000378:metabolism*; D012260:Ribonucleases / Q000737:chemistry / Q000378:metabolism*; D013237:Stereoisomerism
D011392:Proline; D012260:Ribonucleases; C046366:angiogenin; D012259:Ribonuclease, Pancreatic; C058703:ranpirnase