Molecular Life Sciences

Living Edition
| Editors: Robert D. Wells, Judith S. Bond, Judith Klinman, Bettie Sue Siler Masters, Ellis Bell

Forces Maintaining the Stability of Tertiary Structure

Living reference work entry
DOI: https://doi.org/10.1007/978-1-4614-6436-5_16-2

Synonyms

Synopsis

The tertiary structures of proteins are stabilized by intermolecular forces; the hydrophobic effect, hydrogen bonds, ionic interactions, and London dispersion forces all contribute. The relative contribution of these forces has been quantified. More recently, the strategies employed by thermophilic proteins, which allow them to maintain their structures at extreme temperatures, have been identified. A growing appreciation of the need for some proteins to change their tertiary structure has developed, and the factors which allow them to adopt radically different folds are being identified.

Introduction

In order to understand both the stability of protein structure and also their inherent plasticity, it is necessary to understand the transient forces that fold and hold the linear protein chain into a three-dimensional shape. Although these forces are often within an...

Keywords

Tertiary Structure Quaternary Structure Intermolecular Force Hydrophobic Effect Normal Boiling Point 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Springer Science+Business Media New York 2014

Authors and Affiliations

  1. 1.Department of Chemistry and BiochemistrySt. Cloud State UniversitySt. CloudUSA