ISSN:
1573-4943
Keywords:
Protein folding
;
transition-state structure
;
ligand binding
;
ribonuclease mutant
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract The refolding kinetics of guanidine-denatured disulfide-intact bovine pancreatic ribo-nuclease A (RNase A) and its proline-42-to-alanine mutant (Pro42Ala) have been studied by monitoring tyrosine burial and 2′-cytidine monophosphate (2′CMP) inhibitor binding. The folding rate for wild-type RNase A is faster in the presence of the inhibitor 2′CMP than in its absence, indicating that the transition-state structure in the rate-determining step is stabilized by 2′CMP. The folding rate monitored by 2′CMP binding to the major slow-folding species of Pro42Ala RNase A is faster than the folding rate monitored by tyrosine burial; however, the folding rate monitored by inhibitor binding to the minor slow-folding species is decreased significantly over the folding rate monitored by tyrosine burial, indicating that the major and minor slow-folding species of Pro42Ala fold to the native state with different transition-state conformations in the rate-determining step.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01901697
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