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Designing Protein Denaturants: Synthetic Agents Induce Cytochrome c Unfolding at Low Concentrations and Stoichiometries
Author(s) -
Jain Rishi K.,
Hamilton Andrew D.
Publication year - 2002
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20020215)41:4<641::aid-anie641>3.0.co;2-1
Subject(s) - chemistry , stoichiometry , cytochrome c , denaturation (fissile materials) , biophysics , cytochrome , biochemistry , stereochemistry , biology , enzyme , organic chemistry , nuclear chemistry , mitochondrion
The structural diversity and marginal stability (5–15 kcal mol −1 ) of proteins suggest the development of synthetic agents that selectively promote denaturation at low concentrations (see scheme). It is shown that an artificial receptor that binds tightly to the surface of native cytochrome c (cyt. c ) lowers the melting temperature of the protein by 20°C at stoichiometric amounts; the receptor also selectively binds the native form rather than cyt. C551 and surface‐modified cyt. c.