Influence of 63Ser phosphorylation and dephosphorylation on the structure of the stathmin helical nucleation sequence: A molecular dynamics study

Biochemistry

Volumn 51, Issue 42, 2012, Pages 8455-8463

  Missimer, John H ^a   Steinmetz, Michel O ^a   Van Gunsteren, Wilfred F ^b   Dolenc, Jožica ^b,c  

^a PAUL SCHERRER INSTITUTE   (Switzerland)

^b ETH ZURICH   (Switzerland)

^c UNIVERSITY OF LJUBLJANA   (Slovenia)

Author keywords

[No Author keywords available]

Indexed keywords

ATOMIC RESOLUTION; DEPHOSPHORYLATIONS; DISORDERED PROTEINS; EXPERIMENTAL OBSERVATION; EXPERIMENTAL STUDIES; GROMOS FORCE FIELDS; HELICAL CONFIGURATION; HELICAL CONFORMATION; HELICAL STRUCTURES; KEY REGULATORS; MICROTUBULE DYNAMICS; MICROTUBULES; MOLECULAR DYNAMICS SIMULATIONS; NEUTRAL PH; OXYGEN ATOM; PROTEIN-PROTEIN INTERACTIONS; ROOM TEMPERATURE; SALT BRIDGES; SECONDARY STRUCTURES; SIDE-CHAINS; STATHMIN;

MOLECULAR DYNAMICS; NUCLEATION; PEPTIDES;

PHOSPHORYLATION;

SERINE; STATHMIN; TUBULIN;

ARTICLE; BINDING KINETICS; CELL PROLIFERATION; DOWN REGULATION; HYDROGEN BOND; MICROTUBULE; MOLECULAR DYNAMICS; PH; PRESSURE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEPHOSPHORYLATION; PROTEIN INTERACTION; PROTEIN PHOSPHORYLATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; QUANTITATIVE ANALYSIS; ROOM TEMPERATURE; SEQUENCE ANALYSIS; SOLVATION; STRUCTURE ACTIVITY RELATION;

MOLECULAR DYNAMICS SIMULATION; PEPTIDE FRAGMENTS; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; STATHMIN;

EID: 84867769941     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300885y     Document Type: Article

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