title: Implications of macromolecular crowding for protein assembly.
abstract: Recent studies have led to increased appreciation of the influence of excluded volume in solutions of high total macromolecular content ('macromolecular crowding') upon the various classes of reaction that lead to the assembly of proteins and protein complexes. In general, crowding is expected to stabilize native protein structure relative to less compact non-native structures and to favor the formation of functional complexes of native proteins. Under certain pathological conditions, 'overcrowding' may enhance the formation of nonfunctional aggregates of non-native protein (e.g. amyloid and inclusion bodies).
authors.affiliation: Laboratory of Biochemistry and Genetics, Section on Physical Biochemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830, USA. minton@helix.nih
authors.forename: A P
authors.initials: AP
authors.lastname: Minton
mesh_terms: D000255:Adenosine Triphosphate / Q000502:physiology; D000682:Amyloid / Q000378:metabolism; D000818:Animals; D001704:Biopolymers; D048429:Cell Size; D006801:Humans; D046911:Macromolecular Substances; D008954:Models, Biological; D019636:Neurodegenerative Diseases / Q000378:metabolism; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D000682:Amyloid; D001704:Biopolymers; D046911:Macromolecular Substances; D010455:Peptides; D000255:Adenosine Triphosphate