HIV maturation requires multiple cleavage of long polyprotein chains into functional proteins
that include the viral protease itself. Initial cleavage by the protease dimer occurs from within …

Abstract In the Gag-Pol polyprotein of HIV-1, the 99-amino acid protease is flanked at its N-
terminus by a transframe region (TFR) composed of the transframe octapeptide (TFP) and …

Background: 1 H and 15 N transverse relaxation measurements on perdeuterated proteins
are ideally suited for detecting backbone conformational fluctuations on the millisecond …

We report unrestrained, all-atom molecular dynamics simulations of HIV-1 protease that
sample large conformational changes of the active site flaps. In particular, the unliganded …

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 …

We present the first solution structure of the HIV-1 protease monomer spanning the region
Phe 1–Ala 95 (PR 1–95). Except for the terminal regions (residues 1–10 and 91–95) that are …

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 …

Spontaneous mutations at numerous sites distant from the active site of human
immunodeficiency virus type 1 protease enable resistance to inhibitors while retaining …

HIV-1 protease (PR) is a major drug target in combating AIDS, as it plays a key role in
maturation and replication of the virus. Six FDA-approved drugs are currently in clinical use …

Human immunodeficiency virus Type-1 (HIV-1) protease is crucial for viral maturation and
infectivity. Studies of protease dynamics suggest that the rearrangement of the hydrophobic …