ISSN:
1573-4951
Keywords:
Molecular dynamics
;
Thermodynamic cycle-perturbation method
;
Binding free energy
;
Human rhinovirus
;
Antiviral agent binding
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Summary Molecular dynamics simulations have been used to study the free energy of binding of an antiviral agent to the human rhinovirus HRV-14 and to a mutant in which a valine residue in the antiviral binding pocket is replaced by leucine. The simulations predict that the antiviral should bind to the two viruses with similar affinity, in apparent disagreement with experimental results. Possible origins of this discrepancy are outlined. Of particular importance is the apparent need for methods to systematically sample all significant conformations of the leucine side chain.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01532989
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