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Osmolyte-induced Protein Folding Free Energy Changes by Peng Wu; D.W. Bolen is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract Upon addition of protecting osmolyte to an aqueous solution of an intrinsically unstructured protein, spectral observables are often seen to change in a sigmoid fashion as a function of increasing osmolyte concentration. Commonly, such data are analyzed using the linear extrapolation model (LEM), a method that defines a scale from 0%–100% folded species at each osmolyte concentration by means of extending pre‐ and post‐folding baselines into the transition region. Defining the 0%–100% folding scale correctly for each osmolyte is an important part of the analysis, leading to evaluation of the fraction of folded protein existing in the absence of osmolytes. In this study, we used reduced and carboxyamidated RNase T1 (RCAM‐T1) as an intrinsically unstructured protein, and determined the thermodynamic stability of RCAM‐T1 induced by naturally occurring osmolytes. Because the folded fraction of the protein population determined by experiments of thermal and urea‐induced denaturation is nonzero in the absence of osmolytes at 15°C, the commonly used LEM can lead to false values of Δ__G__ for protein folding due to the arbitrary assumption that the protein is 100% unfolded in t

Who reads Osmolyte-induced Protein Folding Free Energy Changes?

Author

Peng Wu; D.W. Bolen

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

2006

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)