Journal
ANNUAL REVIEW OF BIOPHYSICS
Volume 37, Issue -, Pages 375-397Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev.biophys.37.032807.125817
Keywords
excluded volume; configurational entropy; free energy; protein-protein interactions; protein folding; site-binding
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Funding
- Intramural NIH HHS [ZIA DK024957-03, Z01 DK024957-02, Z01 DK024957-01] Funding Source: Medline
- NIGMS NIH HHS [R01 GM058187, GM058187, R01 GM058187-09] Funding Source: Medline
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [ZIADK024957] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM058187] Funding Source: NIH RePORTER
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Expected and observed effects of volume exclusion on the free energy of rigid and flexible macromolecules in crowded and confined systems, and consequent effects of crowding and confinement on macromolecular reaction rates and equilibria are summarized. Findings from relevant theoretical/simulation and experimental literature published from 2004 onward are reviewed. Additional complexity arising from the heterogeneity of local environments in biological media, and the presence of nonspecific interactions between macromolecules over and above steric repulsion, are discussed. Theoretical and experimental approaches to the characterization of crowding and confinement-induced effects in systems approaching the complexity of living organisms are suggested.
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