Resistant mechanism against nelfinavir of subtype C human immunodeficiency virus type 1 proteases

Protein folding: Understanding the role of water and the low Reynolds number environment as the peptide chain emerges from the ribosome and folds

“…These mutants and polymorphisms only affect the final structure or very latest stage of protein folding and fall into two categories. First is the active site mutation, D30N, which has several diverse effects (Soares et al, 2010) and particularly affects the hydrogen bonding between aspartate-30 and the drug (Ode et al, 2005;Moseby et al, 2008;Liu et al, 2011). Second are the non-active site mutations that affect the interaction between these residues and those residues lining the active site binding pocket (Ode et al, 2005(Ode et al, , 2007, mainly by small effects on late folding that distort and reduce the size of the binding pocket, affect the flap and in some cases actually restore the hydrogen binding between the drug and the protein.…”