Molecular Life Sciences

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

Allostery and Quaternary Structure

Living reference work entry
DOI: https://doi.org/10.1007/978-1-4614-6436-5_22-1

Synopsis

Quaternary proteins are multisubunit proteins held in relation to each other through non-covalent forces. Allosteric proteins have another site which binds an effector molecule. The allosteric site ligand binding influences the binding of substrate in a positive or negative (inhibitory) manner. The presence of sigmoidal (as opposed to hyperbolic) kinetics is a valuable clue in the identification of an allosteric protein. Much of our understanding of cooperativity comes from the study of hemoglobin. Ligand binding induces conformational changes in a protein which historically have been investigated using X-ray crystallography. Two models (MWC and KNF) are used to relate conformational change and function. As additional allosteric proteins are studied and new techniques are applied, some long-standing assumptions are being challenged in the absolute, though the assumptions remain true in the general.

Introduction

Quaternary proteins are proteins in which two or more polypeptides...

Keywords

Electrophoresis Lysine Oligomer Polypeptide Histidine 
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Copyright information

© Springer Science+Business Media New York 2014

Authors and Affiliations

  1. 1.Department of ChemistryFort Hays State UniversityHaysUSA