The Use of Chemical Double‐Mutant Cycles in Biomolecular Recognition Studies: Application to HCV NS3 Protease Inhibitors | Zendy

Kawai Stephen H. | Zendy; Bailey Murray D. | Zendy; Halmos Ted | Zendy; Forgione Pat | Zendy; LaPlante Steven R. | Zendy; LlinàsBrunet Montse | Zendy; Naud Julie | Zendy; Goudreau Natalie | Zendy

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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.

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