Role of Electrostatic Interactions in Binding of Peptides and Intrinsically Disordered Proteins to Their Folded Targets: 2. the Model of Encounter Complex Involving the Double Mutant of the c-Crk N-SH3 Domain and Peptide Sos

Biochemistry

Volumn 55, Issue 12, 2016, Pages 1784-1800

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

^a PURDUE UNIVERSITY   (United States)

^b ST PETERSBURG STATE UNIVERSITY   (Russian Federation)

^c UNIVERSITY OF TORONTO   (Canada)

^d DUKE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ARGININE; BIOCHEMISTRY; ELECTROSTATICS; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; SYSTEMS ENGINEERING;

CONFORMATIONAL MOBILITY; DYNAMIC INTERACTION; EMPIRICAL FORCE FIELDS; ENCOUNTER COMPLEX; EQUILIBRIUM DISTANCES; INTRINSICALLY DISORDERED PROTEINS; MOLECULAR DYNAMICS SIMULATIONS; TEMPERATURE COEFFICIENT;

PEPTIDES;

AMINO ACID; INTRINSICALLY DISORDERED PROTEIN; MUTANT PROTEIN; PEPTIDE; PEPTIDE SOS; UNCLASSIFIED DRUG; ONCOPROTEIN; PEPTIDE FRAGMENT; PROTEIN BINDING;

ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; MODEL; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MUTAGENESIS; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; STATIC ELECTRICITY; CHEMISTRY; METABOLISM; MUTATION; PHYSIOLOGY; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

INTRINSICALLY DISORDERED PROTEINS; MUTATION; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-CRK; STATIC ELECTRICITY;

EID: 84962433266     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b01283     Document Type: Article

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