A Thermodynamic Scale for the .beta.-Sheet Forming Tendencies of the Amino Acids
作者： Catherine K. Smith , Jane M. Withka , Lynne Regan
DOI: 10.1021/BI00184A020
关键词:
摘要: The results of a study to measure the beta-sheet forming propensities 20 naturally occurring amino acids are presented. protein host for these studies is 56 acid B1 domain staphylococcal IgG binding G [Fahnestock, S.R., Alexander, P., Nagle, J., & Filpula, D. (1986) J. Bacteriol. 167, 870-880]. This was selected because it exhibits reversible two-state thermal denaturation transition and its structure known at high resolution. A suitable guest position in identified, neighboring environment modified minimize potential artifactual interactions. All were individually substituted site, their effect on protein's stability determined. NMR used verify structural integrity several proteins with different substitutions site. provide thermodynamic scale relative that shows clear correlation preferences derived from statistical surveys structure.
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