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| {{STRUCTURE_1ymr| PDB=1ymr | SCENE= }} | | {{STRUCTURE_1ymr| PDB=1ymr | SCENE= }} |
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| '''The study of reductive unfolding pathways of RNase A (Y92A mutant)'''
| | ===The study of reductive unfolding pathways of RNase A (Y92A mutant)=== |
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| ==Overview==
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| Reductive unfolding studies of proteins are designed to provide information about intramolecular interactions that govern the formation (and stabilization) of the native state and about folding/unfolding pathways. By mutating Tyr92 to G, A, or L in the model protein, bovine pancreatic ribonuclease A, and through analysis of temperature factors and molecular dynamics simulations of the crystal structures of these mutants, it is demonstrated that the markedly different reductive unfolding rates and pathways of ribonuclease A and its structural homologue onconase can be attributed to a single, localized, ring-stacking interaction between Tyr92 and Pro93 in the bovine variant. The fortuitous location of this specific stabilizing interaction in a disulfide-bond-containing loop region of ribonuclease A results in the localized modulation of protein dynamics that, in turn, enhances the susceptibility of the disulfide bond to reduction leading to an alteration in the reductive unfolding behavior of the homologues. These results have important implications for folding studies involving topological determinants to obtain folding/unfolding rates and pathways, for protein structure-function prediction through fold recognition, and for predicting proteolytic cleavage sites.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16433537}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16433537 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16433537}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Xu, G.]] | | [[Category: Xu, G.]] |
| [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:31:08 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:32:55 2008'' |
