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• W2128106046 abstract "An invariant substructure that forms two interlocked pairs of neighboring beta-strands occurs in essentially all known sandwich-like proteins. Eight conserved positions in these strands were recently shown to act as structural determinants. To test whether the residues at these invariant positions are conserved for mechanistic (i.e., part of folding nucleus) or energetic (i.e., governing native-state stability) reasons, we characterized the folding behavior of eight point-mutated variants of the sandwich-like protein Pseudomonas aeruginosa apo-azurin. We find a simple relationship among the conserved positions: half of the residues form native-like interactions in the folding transition state, whereas the others do not participate in the folding nucleus but govern high native-state stability. Thus, evolutionary preservation of these specific positions gives both mechanistic and energetic advantages to members of the sandwich-like protein family." @default.
• W2128106046 created "2016-06-24" @default.
• W2128106046 creator A5051928700 @default.
• W2128106046 creator A5063954863 @default.
• W2128106046 date "2005-03-07" @default.
• W2128106046 modified "2023-09-27" @default.
• W2128106046 title "Role of structural determinants in folding of the sandwich-like protein <i>Pseudomonas aeruginosa</i> azurin" @default.
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• W2128106046 doi "https://doi.org/10.1073/pnas.0501038102" @default.
• W2128106046 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/554837" @default.
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