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Modern Thermodynamics for Chemists and Biochemists$
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Dennis Sherwood and Paul Dalby

Print publication date: 2018

Print ISBN-13: 9780198782957

Published to Oxford Scholarship Online: August 2018

DOI: 10.1093/oso/9780198782957.001.0001

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Macromolecular conformations and interactions

Macromolecular conformations and interactions

Chapter:
(p.747) 25 Macromolecular conformations and interactions
Source:
Modern Thermodynamics for Chemists and Biochemists
Author(s):

Dennis Sherwood

Paul Dalby

Publisher:
Oxford University Press
DOI:10.1093/oso/9780198782957.003.0025

As a polymer of many amino acids, any given protein can, in principle, adopt a huge number of configurations. In reality, however, the biologically stable protein adopts a single configuration that is stable over time. Thermodynamically, this configuration must represent a Gibbs free energy minimum. This chapter therefore explores how the thermodynamics and kinetics of protein folding and unfolding can be investigated experimentally (using, for example, chaotropes, heating or ligand interactions), and how these measurements can be used to enrich our understanding of protein configurations and stability.

Keywords:   protein, primary structure, secondary structure, tertiary structure, quaternary structure, folding, unfolding, protein stability, chaotrope, thermal unfolding, ligand, protein-ligand interaction, binding isotherm, protein folding kinetics, Levinthal’s paradox, transition state theory, mutation, phi-value analysis, protein folding pathway

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