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Protein stability curves
Author(s) -
Becktel Wayne J.,
Schellman John A.
Publication year - 1987
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360261104
Subject(s) - chemistry , denaturation (fissile materials) , thermodynamics , stability (learning theory) , protein stability , equilibrium unfolding , heat capacity , constant (computer programming) , function (biology) , melting temperature , protein folding , crystallography , biochemistry , physics , materials science , composite material , machine learning , evolutionary biology , biology , computer science , nuclear chemistry , programming language
The stability curve of a protein is defined as the plot of the free energy of unfolding as a function of temperature. For most proteins the change in heat capacity on denaturation, or unfolding, is large but approximately constant. When unfolding is s two‐state process, most of the salient features of the stability curves of proteins can be derived from this fact. A number of relations are obtained, including the special features of low‐temperature denaturation, the properties of the maximum in stability, and the interrelationships of the characteristic temperatures of the protein. The paper closes with a formula that permits one to calculate small changes in stabilization free energy from changes in the melting temperature of the protein.