Drug resistance of mutations in HIV-1 protease (PR) badly reduce the efficiency of the
current inhibitors in clinical treatments of AIDS. In this work, molecular dynamics (MD) …

Even though more than 200 three‐dimensional structures of HIV‐1 protease complexed to a
variety of inhibitors are available in the Protein Data Bank; very few structures of unliganded …

NMR and MD simulations have demonstrated that the flaps of HIV-1 protease (HIV-1p) adopt
a range of conformations that are coupled with its enzymatic activity. Previously, a model …

The conformational dynamics in the flaps of HIV-1 protease plays a crucial role in the
mechanism of substrate binding. We develop a kinetic network model, constructed from …

The crystal structures, dimer stabilities, and kinetics have been analyzed for wild-type
human immunodeficiency virus type 1 (HIV-1) protease (PR) and resistant mutants PRL24I …

Drug resistance has sharply limited the effectiveness of HIV-1 protease inhibitors in AIDS
therapy. It is critically important to understand the basis of this resistance for designing new …

We investigated the HIV-1 protease molecule for the occurrence of cooperative folding units,
ie structural units that exhibit a relatively stronger protection against unfolding than do other …

A structural parametrization of the binding and folding energetics previously developed in
this laboratory accounts quantitatively for the binding of 13 HIV-1 protease inhibitors for …

Drug resistance is a very important factor contributing to the failure of current HIV therapies.
The ability to understand the resistance mechanism of HIV-protease mutants may be useful …

The flexibility of HIV‐1 protease flaps is known to be essential for the enzymatic activity.
Here we attempt to capture a multitude of conformations of the free and substrate‐bound HIV …