HIV-1 protease remains a major target for the design of anti HIV/AIDS drugs. However there are an emergence of drug resistant virus strains that bury mutations within protease gene. In order to study molecular basis of the drug resistance it is essential to understand contribution of point mutations to overall resistance. Distal mutations has little impact on the protease conformation however could effect its molecular dynamics. In present study we investigated effect of Leu10→Ile mutation on molecular dynamics of HIV-1 protease. A 10ns-long trajectory was computed to be further compared with that of wild type protease. A significantly impaired conformational fluctuations of the mutant protease suggests that Leu10→Ile mutation has increased stability of the tertiary structure. Redistribution of the RMS fluctuations along with an alteration of the direction of slow correlated motions of the protease indicate the effect of the Leu10→Ile mutation on molecular dynamics of the HIV-1 protease. Liaison between modified dynamics and drug resistance is discussed.