Temperature effects on the hydrodynamic radius of the intrinsically disordered N-terminal region of the p53 protein

Proteins: Structure, Function and Bioinformatics

Volumn 82, Issue 4, 2014, Pages 668-678

  Langridge, Timothy D ^a   Tarver, Micheal J ^a   Whitten, Steven T ^a  

^a Texas State University   (United States)

Author keywords

Acidic activation domain; Heat; Hydrodynamic radius; Intrinsically disordered protein; Net charge; Polyproline

Indexed keywords

GLYCINE; INTRINSICALLY DISORDERED PROTEIN; POLYPEPTIDE; PROLINE; PROTEIN P53;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; HEAT; HYDRODYNAMIC RADIUS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE; STATISTICAL PARAMETERS; TEMPERATURE DEPENDENCE; TEMPERATURE SENSITIVITY; THERMAL ANALYSIS;

ACIDIC ACTIVATION DOMAIN; HEAT; HYDRODYNAMIC RADIUS; INTRINSICALLY DISORDERED PROTEIN; NET CHARGE; POLYPROLINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CIRCULAR DICHROISM; COMPUTER SIMULATION; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLYCINE; HYDRODYNAMICS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; INTRINSICALLY DISORDERED PROTEINS; MODELS, MOLECULAR; PROLINE; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; TEMPERATURE; TUMOR SUPPRESSOR PROTEIN P53;

EID: 84895548711     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24449     Document Type: Article

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