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• W1995722669 endingPage "788" @default.
• W1995722669 startingPage "780" @default.
• W1995722669 abstract "Abstract The WW domains are known as the smallest naturally occurring, monomeric, triple‐stranded, antiparallel β‐sheet domains. Hence, we chose the FBP28 WW domain as a model to investigate the stability of the β‐sheet structure at the amino acid level in the context of its function (ligand binding). The structure–function relationship was investigated through a complete substitution analysis of the FBP28 WW domain, with variants synthesized as a cellulose‐bound peptide array. The functionality of the FBP28 WW domain variants was examined by probing the peptide array for ligand binding. In addition, selected FBP28 WW domain variants were investigated by CD measurements to determine the stability of the antiparallel β‐sheet structure. We discuss the correlation between structure stability and functionality for the FBP28 WW domain, as well as the effect of ligand‐induced structure stabilization." @default.
• W1995722669 created "2016-06-24" @default.
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• W1995722669 date "2006-04-26" @default.
• W1995722669 modified "2023-10-16" @default.
• W1995722669 title "Probing the Ligand-Binding Specificity and Analyzing the Folding State of SPOT-Synthesized FBP28 WW Domain Variants" @default.
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• W1995722669 doi "https://doi.org/10.1002/cbic.200500408" @default.
• W1995722669 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16575938" @default.
• W1995722669 hasPublicationYear "2006" @default.
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