Role of tyrosine hot-spot residues at the interface of colicin E9 and immunity protein 9: A comparative free energy simulation study

Proteins: Structure, Function and Bioinformatics

Volumn 81, Issue 3, 2013, Pages 461-468

  Luitz, Manuel P ^a   Zacharias, Martin ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

Alchemical transformation; Colicin immunity protein interaction; Free energy calculations; Hot spot interface residues; Molecular dynamic simulations

Indexed keywords

ALANINE; COLICIN; COLICIN E9; IMMUNITY PROTEIN 9; ISOLEUCINE; LEUCINE; PROTEIN; SERINE; SOLVENT; TYROSINE; UNCLASSIFIED DRUG; VALINE;

ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; ENERGY YIELD; HYDRATION; MOLECULAR DYNAMICS; MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; SIMULATION; SOLVATION;

ALANINE; ALGORITHMS; AMINO ACID SUBSTITUTION; COLICINS; ENERGY METABOLISM; MOLECULAR DYNAMICS SIMULATION; MULTIPROTEIN COMPLEXES; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN INTERACTION MAPPING; SOLVENTS; STATIC ELECTRICITY; TYROSINE;

BACTERIA (MICROORGANISMS);

EID: 84873097928     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24203     Document Type: Article

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