Models for excluded volume interaction between an unfolded protein and rigid macromolecular cosolutes: Macromolecular crowding and protein stability revisited

Biophysical Journal

Volumn 88, Issue 2, 2005, Pages 971-985

  Minton, Allen P ^a,b  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

POLYMER; POLYPEPTIDE; PROTEIN; RIBONUCLEASE A; MULTIPROTEIN COMPLEX; PANCREATIC RIBONUCLEASE; PEPTIDE; UREA;

ARTICLE; MACROMOLECULE; MATHEMATICAL MODEL; MOLECULAR INTERACTION; MONTE CARLO METHOD; PARTICLE SIZE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; THERMODYNAMICS; BINDING SITE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER SIMULATION; DRUG MIXTURE; ENZYME STABILITY; EVALUATION; METHODOLOGY; MICROFLUIDICS; PROTEIN BINDING; SOLUBILITY; STATISTICAL MODEL; STRUCTURE ACTIVITY RELATION; VALIDATION STUDY;

BINDING SITES; COMPLEX MIXTURES; COMPUTER SIMULATION; ENZYME STABILITY; MICROFLUIDICS; MODELS, CHEMICAL; MODELS, MOLECULAR; MODELS, STATISTICAL; MULTIPROTEIN COMPLEXES; PEPTIDES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEINS; RIBONUCLEASE, PANCREATIC; SOLUBILITY; STRUCTURE-ACTIVITY RELATIONSHIP; UREA;

EID: 16344364032     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.050351     Document Type: Article

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