Inclusion of ionization states of ligands in affinity calculations

Proteins: Structure, Function and Bioinformatics

Volumn 76, Issue 1, 2009, Pages 138-150

  Donnini, Serena ^a   Villa, Alessandra ^b   Groenhof, Gerrit ^c   Mark, Alan E ^d   Wierenga, Rik K ^a   Juffer, André H ^a,c  

^a UNIVERSITY OF OULU   (Finland)

^b MAX PLANCK INSTITUTE FOR POLYMER RESEARCH   (Germany)

^c MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^d UNIVERSITY OF QUEENSLAND   (Australia)

Author keywords

Binding free energy; Effective affinity; Molecular dynamics; pK calculations; Protonation equilibria; Thermodynamic integration; Triosephosphate isomerase

Indexed keywords

2 PHOSPHOGLYCOLATE; 3 PHOSPHONOPROPIONIC ACID; GLYCOLIC ACID DERIVATIVE; LIGAND; PHOSPHONIC ACID DERIVATIVE; TRIOSEPHOSPHATE ISOMERASE; UNCLASSIFIED DRUG;

AB INITIO CALCULATION; ARTICLE; BINDING AFFINITY; ENERGY; ENZYME ACTIVE SITE; ENZYME BINDING; IONIZATION; LIGAND BINDING; MOLECULAR DYNAMICS; PKA; PRIORITY JOURNAL; PROTON TRANSPORT; SIMULATION; SOLVATION;

EID: 84962343568     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22326     Document Type: Article

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