Theoretical IR spectroscopy based on QM/MM calculations provides changes in charge distribution, bond lengths, and bond angles of the GTP ligand induced by the Ras-protein

Biophysical Journal

Volumn 88, Issue 6, 2005, Pages 3829-3844

  Klähn, Marco ^a,b   Schlitter, Jürgen ^a   Gerwert, Klaus ^a  

^a RUHR UNIVERSITY BOCHUM   (Germany)

^b UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA PHOSPHATE; BETA PHOSPHATE; GAMMA PHOSPHATE; GLYCINE; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; LIGAND; LYSINE; MAGNESIUM ION; PHOSPHATE; RAS P21 PROTEIN; RAS PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BOND ANGLE; BOND LENGTH; CALCULATION; CATALYSIS; CONFORMATION; COVALENT BOND; DENSITY FUNCTIONAL THEORY; ELECTRICITY; ENERGY; ENZYME SUBSTRATE COMPLEX; FREE ACTIVATION ENERGY; INFRARED SPECTROSCOPY; MOLECULAR MECHANICS; QUANTUM MECHANICS; SIGNAL TRANSDUCTION; VIBRATION;

EID: 22244451654     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.058644     Document Type: Article

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