Order through disorder: Hyper-mobile C-terminal residues stabilize the folded state of a helical peptide. A molecular dynamics study

PLoS ONE

Volumn 5, Issue 12, 2010, Pages

  Patapati, Kalliopi K ^a   Glykos, Nicholas M ^a  

^a DEMOCRITUS UNIVERSITY OF THRACE   (Greece)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; GLYCINE; LYSINE; LACTALBUMIN; PEPTIDE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENERGY TRANSFER; GENE DELETION; MOLECULAR DYNAMICS; PEPTIDE ANALYSIS; PROCESS MODEL; PROTEIN CONFORMATION; PROTEIN DEFECT; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; THERMODYNAMICS; THERMOSTABILITY; ALGORITHM; CHEMISTRY; COMPUTER PROGRAM; COMPUTER SIMULATION; HUMAN; PRINCIPAL COMPONENT ANALYSIS; PROTEIN TERTIARY STRUCTURE; STATIC ELECTRICITY; TEMPERATURE;

ALGORITHMS; COMPUTER SIMULATION; HUMANS; LACTALBUMIN; MOLECULAR DYNAMICS SIMULATION; PEPTIDES; PRINCIPAL COMPONENT ANALYSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SOFTWARE; STATIC ELECTRICITY; TEMPERATURE; THERMODYNAMICS;

EID: 78650880629     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0015290     Document Type: Article

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