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The Use of Chemical Double‐Mutant Cycles in Biomolecular Recognition Studies: Application to HCV NS3 Protease Inhibitors
Author(s) -
Kawai Stephen H.,
Bailey Murray D.,
Halmos Ted,
Forgione Pat,
LaPlante Steven R.,
LlinàsBrunet Montse,
Naud Julie,
Goudreau Natalie
Publication year - 2008
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.200800214
Subject(s) - ns3 , protease , mutant , computational biology , hepatitis c virus , chemistry , protease inhibitor (pharmacology) , ligand (biochemistry) , virology , biochemistry , biology , enzyme , virus , receptor , gene , antiretroviral therapy , viral load
Things don′t always add up : Our understanding of biomolecular recognition processes is often complicated by the fact that the binding contributions of individual ligand–protein subcontacts do not add up in a linear fashion. Chemical double‐mutant cycles are useful analyses to quantify the degree of nonadditivity in such binding phenomena, and peptidyl inhibitors of hepatitis C virus NS3 protease are used to exemplify this.