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Noncovalent Forces Important to the Conformational Stability of Protein Structures

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Protein Stability and Folding

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

Abstract

Proteins are the workhorses of life, responsible for catalyzing the numerous chemical reactions necessary to living cells as well as being important structural molecules. The functionality of proteins requires the correct spatial placement of amino acid side chains and prosthetic groups that, in turn, requires a defined three-dimensional structure of the protein chain. The three-dimensional structure is obtained through the folding of the polypeptide chain from an ensemble of fairly loose, disordered con figurations, collectively referred to as the unfolded state, into a well-defined compact configuration, known as the native state.

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Authors and Affiliations

  1. Department of Biochemistry, University of Iowa, Iowa City, IA

    Kenneth P. Murphy

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  1. Kenneth P. Murphy
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Editors and Affiliations

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

    Bret A. Shirley

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Murphy, K.P. (1995). Noncovalent Forces Important to the Conformational Stability of Protein Structures. In: Shirley, B.A. (eds) Protein Stability and Folding. Methods in Molecular Biology™, vol 40. Humana Press. https://doi.org/10.1385/0-89603-301-5:1

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  • DOI: https://doi.org/10.1385/0-89603-301-5:1

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-301-6

  • Online ISBN: 978-1-59259-527-3

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