Studies from Hebrew University, Institute of Chemistry have provided new information about HIV/AIDS.

A new study, 'The C-terminal domain of the HIV-1 Vif protein is natively unfolded in its unbound state,' is now available. According to a study from Givat Ram, Israel, "The human immunodeficiency virus type-1 (HIV-1) Vif protein neutralizes the cellular defense mechanism against the virus. The C-terminal domain of Vif (CTD, residues 141-192) mediates many of its interactions."

"Full-length Vif is difficult to purify in large amounts, hence the only available structure of Vif is of residues 140-155 within the ElonginBC complex. Other structural information, derived from modeling and indirect experiments, indicates that the Vif CTD may be unstructured. Here, we …