Exploring the protein G helix free-energy surface by solute tempering metadynamics

Proteins: Structure, Function and Genetics

Volumn 71, Issue 4, 2008, Pages 1647-1654

  Camilloni, Carlo ^a,b   Provasi, Davide ^a,b   Tiana, Guido ^a,b,d   Broglia, Ricardo A ^a,b,c  

^a UNIVERSITY OF MILAN   (Italy)

^b INFN SEZIONE DI MILANO   (Italy)

^c UNIVERSITY OF COPENHAGEN   (Denmark)

^d Department of Physics ^*  (Italy)

Author keywords

helix; helix; Free energy surface; Metadynamics; Protein G; Solute tempering

Indexed keywords

PROTEIN G;

ALGORITHM; ALPHA HELIX; ARTICLE; ENERGY; HYDROPHOBICITY; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN MOTIF; PROTEIN STABILITY; PROTEIN STRUCTURE; SOLUTE; THERMODYNAMICS;

ALGORITHMS; AMINO ACID SEQUENCE; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; COMPUTER SIMULATION; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; HYDROPHOBICITY; KINETICS; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; NERVE TISSUE PROTEINS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SOLVENTS; TEMPERATURE; THERMODYNAMICS; WATER;

EID: 44349186795     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21852     Document Type: Article

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