Native-like folding intermediates of homologous ribonucleases.
The mechanism of the slow refolding reactions of four different pancreatic ribonucleases from ox, sheep, red deer, and roe deer has been investigated. Refolding kinetics of these proteins were very similar. In particular, a native-like intermediate, IN, was shown to be populated on the slow refolding pathway of all ribonucleases. We conclude that, similar to the stability of the folded proteins, the pathway of slow refolding has been conserved despite the differences in amino acid sequence and the varying number of proline residues.
D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D003670:Deer; D019791:Guanidine; D006146:Guanidines / Q000494:pharmacology; D007700:Kinetics; D011487:Protein Conformation; D012259:Ribonuclease, Pancreatic / Q000378:metabolism; D012260:Ribonucleases / Q000302:isolation & purification / Q000378:metabolism*; D012756:Sheep; D013045:Species Specificity; D013050:Spectrometry, Fluorescence; D014443:Tyrosine / Q000032:analysis
D006146:Guanidines; D014443:Tyrosine; D012260:Ribonucleases; D012259:Ribonuclease, Pancreatic; D019791:Guanidine