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• W2040783467 startingPage "259" @default.
• W2040783467 abstract "The focal adhesion target (FAT) domain of focal adhesion kinase has a four-helix bundle structure. Based on a hydrogen exchange-constrained computer simulation study and some indirect experimental results, it has been suggested that a partially unfolded state of the FAT domain with the N-terminal helix unfolded plays an important role in its biological function. Here, using a native-state hydrogen exchange method, we directly detected an intermediate with the N-terminal helix unfolded in a mutant (Y925E) of the FAT domain. In addition, kinetic folding studies on the FAT domain suggest that this intermediate exists on the native side of the rate-limiting transition state for folding. These results provide more direct evidence of the existence of the proposed intermediate and help to understand the folding mechanism of small single domain proteins." @default.
• W2040783467 created "2016-06-24" @default.
• W2040783467 creator A5053210714 @default.
• W2040783467 creator A5069137667 @default.
• W2040783467 creator A5072545375 @default.
• W2040783467 date "2006-08-14" @default.
• W2040783467 modified "2023-10-10" @default.
• W2040783467 title "Detection of a hidden folding intermediate in the focal adhesion target domain: Implications for its function and folding" @default.
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• W2040783467 doi "https://doi.org/10.1002/prot.21107" @default.
• W2040783467 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16909417" @default.
• W2040783467 hasPublicationYear "2006" @default.
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