Role of electrostatic interactions in binding of peptides and intrinsically disordered proteins to their folded targets. 1. NMR and MD characterization of the complex between the c-Crk N-SH3 domain and the peptide sos

Biochemistry

Volumn 53, Issue 41, 2014, Pages 6473-6495

  Xue, Yi ^a   Yuwen, Tairan ^a   Zhu, Fangqiang ^b   Skrynnikov, Nikolai R ^a,c  

^a PURDUE UNIVERSITY   (United States)

^b INDIANA UNIVERSITY   (United States)

^c ST PETERSBURG STATE UNIVERSITY   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

AMBER; AMINO ACIDS; ELECTROSTATICS; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; SYSTEMS ENGINEERING;

CONFORMATIONAL STATE; CRYSTALLOGRAPHIC COORDINATES; EQUILIBRIUM DISTANCES; EXPERIMENTAL CHARACTERIZATION; INTRINSICALLY DISORDERED PROTEINS; MAGNETIC FIELD STRENGTHS; MECHANISM OF FORMATION; MOLECULAR DYNAMICS TRAJECTORIES;

PEPTIDES;

CRK LIKE PROTEIN; INTRINSICALLY DISORDERED PROTEIN; NITROGEN; OXYGEN; PROTEIN SH3; SOS PROTEIN; CRK PROTEIN, MOUSE; HYBRID PROTEIN; MUTANT PROTEIN; OLIGOPEPTIDE; ONCOPROTEIN; PEPTIDE FRAGMENT;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; EQUILIBRIUM CONSTANT; HYDROPHOBICITY; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; STATIC ELECTRICITY; AMINO ACID SUBSTITUTION; ANIMAL; BINDING SITE; CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; GENETICS; METABOLISM; MOUSE; PROTEIN CONFORMATION; PROTEIN STABILITY;

AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; INTRINSICALLY DISORDERED PROTEINS; MICE; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; MUTANT PROTEINS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OLIGOPEPTIDES; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STABILITY; PROTO-ONCOGENE PROTEINS C-CRK; RECOMBINANT FUSION PROTEINS; SOS1 PROTEIN; STATIC ELECTRICITY;

EID: 84908155664     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500904f     Document Type: Article

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