title: Globular Protein Folding In Vitro and In Vivo.
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.
authors.affiliation: Center for Biophysics and Quantitative Biology, University of Illinois, Urbana, Illinois 61801; email: mgruebel@illinois.edu , kapildave91@gmail.com.|Department of Chemistry, University of Illinois, Urbana, Illinois 61801; email: shaharsu@gmail.com.|Department of Physics, University of Illinois, Urbana, Illinois 61801.
authors.forename: Martin
authors.initials: M
authors.lastname: Gruebele
authors.affiliation: Center for Biophysics and Quantitative Biology, University of Illinois, Urbana, Illinois 61801; email: mgruebel@illinois.edu , kapildave91@gmail.com.
authors.forename: Kapil
authors.initials: K
authors.lastname: Dave
authors.affiliation: Department of Chemistry, University of Illinois, Urbana, Illinois 61801; email: shaharsu@gmail.com.
authors.forename: Shahar
authors.initials: S
authors.lastname: Sukenik
mesh_terms: D006801:Humans; D007700:Kinetics; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D011506:Proteins
keywords: energy landscape; folding kinetics; folding thermodynamics; free energy; in-cell folding; lattice model; protein evolution; protein function; single molecule