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Protein Stability and Folding pp 253–269Cite as

Solvent Stabilization of Protein Structure

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Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 40))

Abstract

The stability of the native structure of globular proteins is known to be affected strongly by a variety of substances that act at high concentration (usually ≥1M). We will refer to these as co-solvents, whether they are liquids or solids. Some of these substances are known to stabilize protein structure, others to destabilize it, whereas still others can act either as stabilizers or destabilizers, depending on their concentration and on the solution pH (1). The first class encompasses sugars (sucrose, trehalose), glycerol, other polyols (sorbitol, mannitol), some amino acids (glycine, proline), methyl amines (sarcosine, trimethylamine-N-oxide), in fact most osmolytes used by nature (2–4), and also some salting out salts, such as MgS04. The second class consists of the strong denaturants, such as urea, guanidine hydrochloride, and sodium dodecyl sulfate. The last class is composed of weakly acting agents, such as guanidine sulfate (5), MgCl2 (6), the glutamate ion, and dimethyl sulfoxide (DMSO).

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Author information

Authors and Affiliations

  1. Graduate Department of Biochemistry, Brandeis University, Waltham, MA

    Serge N. Timasheff

Authors
  1. Serge N. Timasheff
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Editor information

Editors and Affiliations

  1. Boehringer Ingelheim Pharmaceuticals, Inc., Ridgefield, CT

    Bret A. Shirley

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© 1995 Humana Press Inc.

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Timasheff, S.N. (1995). Solvent Stabilization of Protein Structure. In: Shirley, B.A. (eds) Protein Stability and Folding. Methods in Molecular Biology™, vol 40. Humana Press. https://doi.org/10.1385/0-89603-301-5:253

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  • DOI: https://doi.org/10.1385/0-89603-301-5:253

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-301-6

  • Online ISBN: 978-1-59259-527-3

  • eBook Packages: Springer Protocols

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