Influence of macromolecular crowding upon the stability and state of association of proteins: predictions and observations.
The concept of excluded volume and possible effects of excluded volume on the reactivity of macromolecules in highly volume-occupied or "crowded" media are introduced and briefly summarized. Theoretical and experimental studies of the effect of crowding on protein folding and unfolding, and on the effect of crowding on protein association and aggregation, are reviewed. Possible effects of the effect of crowding on an initially native protein that can undergo unfolding, self-association of native protein, and/or aggregation of non-native protein are considered.
Minton
Allen P
AP
Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U.S. Public Health Service, Bethesda, MD, USA. minton@helix.nih.gov
D001702:Biopharmaceutics; D004355:Drug Stability; D004795:Enzyme Stability; D005079:Excipients / Q000737:chemistry*; D007700:Kinetics; D046911:Macromolecular Substances / Q000737:chemistry*; D008962:Models, Theoretical; D009113:Muramidase / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
D005079:Excipients; D046911:Macromolecular Substances; D011506:Proteins; D009113:Muramidase