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- W2034227566 abstract "It is now widely recognized that the unfolded state of a protein in equilibrium with the native state under folding conditions may contain significant residual structures. However, due to technical difficulties residue-specific interactions in the unfolded state remain elusive. Here we introduce a method derived from the Wyman-Tanford theory to determine residue-specific pK(a)'s in the unfolded state. This method requires equilibrium stability measurements of the wild type and single-point mutants in which titrable residues are replaced with charge-neutral ones under two pH conditions. Application of the proposed approach reveals a highly depressed pK(a) for Asp8 in the unfolded state of the NTL9 protein. Knowledge of unfolded-state pK(a)'s enables quantitative estimation of the unfolded-state electrostatic effects on protein stability. It also provides valuable benchmarks for the improvement of force fields and validation of microscopic information from molecular dynamics simulations." @default.
- W2034227566 created "2016-06-24" @default.
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- W2034227566 date "2010-05-06" @default.
- W2034227566 modified "2023-09-23" @default.
- W2034227566 title "A Method To Determine Residue-Specific Unfolded-State p<i>K</i><sub>a</sub> Values from Analysis of Stability Changes in Single Mutant Cycles" @default.
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- W2034227566 doi "https://doi.org/10.1021/ja101761m" @default.
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