Natively unfolded protein stability as a coil-to-globule transition in charge/hydropathy space

Journal of the American Chemical Society

Volumn 130, Issue 29, 2008, Pages 9536-9542

  Ashbaugh, Henry S ^a   Hatch, Harold W ^a  

^a Tulane University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADSORPTION; AMINES; CHAIN LENGTH; CONDENSATION; CONFORMATIONS; CORRELATION METHODS; FEES AND CHARGES; FINANCE; FORECASTING; POLYPEPTIDES; PROTEINS; STABILIZATION; SYSTEM STABILITY;

AMERICAN CHEMICAL SOCIETY (ACS); BOUNDARY LINES; COARSE GRAINED (CG); COIL-TO-GLOBULE TRANSITION; COMPOSITION SPACE; CONFORMATIONAL DISORDERS; COUNTER-IONS; COUNTERION ADSORPTION; COUNTERION CONDENSATION; HYDROPHOBIC RESIDUES; INDEPENDENCE (PERSONALITY); INDEPENDENT PREDICTORS; INDEPENDENT STABILITY; PROTEIN SEQUENCING; PROTEIN STABILITY; QUANTITATIVE AGREEMENT; REPULSIVE ELECTROSTATIC INTERACTIONS; SEQUENCE LENGTHS; SIMULATION RESULTS; WIDE-RANGE;

HYDROPHOBICITY;

POLYPEPTIDE;

AMINO ACID SEQUENCE; ARTICLE; ELECTRICITY; HYDROPHOBICITY; MOLECULAR DYNAMICS; PEPTIDE SYNTHESIS; POLYMERIZATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; SIMULATION;

ADSORPTION; COMPUTER SIMULATION; ELECTROSTATICS; HYDROPHOBICITY; MODELS, MOLECULAR; PEPTIDES; PROTEIN FOLDING; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS;

EID: 47749110305     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja802124e     Document Type: Article

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