Globular Protein Folding In Vitro and In Vivo

In vitro, computational, and theoretical studies of protein folding have converged to paint a rich and complex energy landscape. This landscape is sensitively modulated by environmental conditions and subject to evolutionary pressure on protein function. Of these environments, none is more complex t...

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Bibliographic Details
Published inAnnual review of biophysics Vol. 45; p. 233
Main Authors Gruebele, Martin, Dave, Kapil, Sukenik, Shahar
Format Journal Article
LanguageEnglish
Published United States 05.07.2016
Subjects
Humans
Kinetics
Protein Conformation
Protein Folding
Proteins - chemistry
Thermodynamics
energy landscape
single molecule
free energy
protein evolution
lattice model
folding thermodynamics
folding kinetics
protein function
in-cell folding
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Summary:In vitro, computational, and theoretical studies of protein folding have converged to paint a rich and complex energy landscape. This landscape is sensitively modulated by environmental conditions and subject to evolutionary pressure on protein function. Of these environments, none is more complex than the cell itself, where proteins function in the cytosol, in membranes, and in different compartments. A wide variety of kinetic and thermodynamics experiments, ranging from single-molecule studies to jump kinetics and from nuclear magnetic resonance to imaging on the microscope, have elucidated how protein energy landscapes facilitate folding and how they are subject to evolutionary constraints and environmental perturbation. Here we review some recent developments in the field and refer the reader to some original work and additional reviews that cover this broad topic in protein science.
ISSN:1936-1238
DOI:10.1146/annurev-biophys-062215-011236