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Probing the Ligand‐Binding Specificity and Analyzing the Folding State of SPOT‐Synthesized FBP28 WW Domain Variants
Author(s) -
Przezdziak Jana,
Tremmel Sandra,
Kretzschmar Ines,
Beyermann Michael,
Bienert Michael,
VolkmerEngert Rudolf
Publication year - 2006
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200500408
Subject(s) - folding (dsp implementation) , domain (mathematical analysis) , ww domain , ligand (biochemistry) , hot spot (computer programming) , chemistry , computational biology , protein folding , biophysics , biology , crystallography , nanotechnology , materials science , computer science , receptor , biochemistry , gene , engineering , mathematics , electrical engineering , mathematical analysis , operating system
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.