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Biophysical Reviews

, Volume 10, Issue 2, pp 203–208 | Cite as

Protein–solvent interaction

  • Tsutomu Arakawa
Review

Abstract

Protein folding and assembly can be manipulated in in vitro systems by co-solvents at high concentrations. A number of co-solvents that enhance protein stability and assembly have been shown to be excluded from the protein surface. Such co-solvent exclusion has been demonstrated by dialysis experiments and shown to be correlated with their effects on protein stability and assembly.

Keywords

Protein folding and assembly In vitro systems Co-solvents Preferentially excluded co-solvents Dialysis equilibrium 

Notes

Compliance with ethical standards

Conflict of interest

Tsutomu Arakawa declares that he has no conflicts of interest.

Ethical approval

This article does not contain any studies with human participants or animals performed by the author.

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Copyright information

© International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature 2017

Authors and Affiliations

  1. 1.Alliance Protein Laboratories, a Division of KBI BiopharmaSan DiegoUSA

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