[24] Evaluating contribution of hydrogen bonding and hydrophobic bonding to protein folding
Methods in enzymology on CD-ROM/Methods in enzymologyPublished 1 January 1995
C. Nick Pace
Citations83
SJR quartileQ4
SJR score0.13
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TL;DR
The chapter discusses the methods of determining denaturation curves and analyzing the results and discusses the interplay between experimental studies of the type described and theoretical studies that will eventually lead to a good understanding of the forces that contribute to protein stability.
Abstract
Publisher Summary This chapter evaluates contribution of hydrogen bonding and hydrophobic bonding to protein folding. The primary goal of studying hydrophobic mutants is to learn how much stability is gained when a protein buries a nonpolar side chain in folding. The goal of studying hyrogen-bonding mutants is to learn how much stability is gained when a polar group that is hydrogen bonded to water in the unfolded state is dehydrated in protein folding to form an intramolecular hydrogen bond. The interplay between experimental studies of the type described and theoretical studies will eventually lead to a good understanding of the forces that contribute to protein stability. Hydrogen bonding and hydrophobic bonding are thought to be the major forces contributing to the conformational stability of proteins. The techniques most often used to measure the conformational stability of a protein are solvent denaturation curves, which are generally urea or guanidine hydrochloride (GdnHC1), thermal denaturation curves, and differential scanning calorimetry (DSC). The chapter discusses the methods of determining denaturation curves and analyzing the results.
Keywords
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