Globular Protein Folding In Vitro and In Vivo

Author:

Gruebele Martin123,Dave Kapil1,Sukenik Shahar2

Affiliation:

1. Center for Biophysics and Quantitative Biology, University of Illinois, Urbana, Illinois 61801;,

2. Department of Chemistry, University of Illinois, Urbana, Illinois 61801;

3. Department of Physics, University of Illinois, Urbana, Illinois 61801

Abstract

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.

Publisher

Annual Reviews

Subject

Cell Biology,Biochemistry,Bioengineering,Structural Biology,Biophysics

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