HIV/AIDS
New HIV/AIDS study findings have been reported from M.K. Rout et al
Published in AIDS Weekly, April 20th, 2009
According to recent research published in the journal Archives of Biochemistry and Biophysics, "Folding, in-vivo, starts from a denatured state and thus the nature of the denatured state would play an important role in directing the folding of a protein. We report here NMR characterization of the acid-denatured state of a Mutant of HIV-1 protease, designed to prevent autolysis (Q7K, L331, L631) and to prevent cysteine oxidation (C67A and C95A)."
"Secondary chemical shifts, TALOS analysis of chemical shifts and N-15 relaxation data (R-1, R-2, NOE) coupled with AABUF and hydrophobicity calculations, suggest formation of hydrophobic clusters and possibility of some...
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Source: AIDS Weekly (2009-04-20)
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