Literature summary for 3.4.23.16 extracted from

Noel, A.F.; Bilsel, O.; Kundu, A.; Wu, Y.; Zitzewitz, J.A.; Matthews, C.R.
The folding free-energy surface of HIV-1 protease: insights into the thermodynamic basis for resistance to inhibitors (2009), J. Mol. Biol., 387, 1002-1016.

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Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
determination of folding free-energy surface of a pseudo-wild-type variant, by a combination of equilibrium and kinetic experiments on the urea-induced unfolding/refolding reactions. Data reveal the presence of a fully folded monomeric intermediate that associates to form the native dimeric structure, with the presence of a transient intermediate in the monomer folding reaction. The partially folded and fully folded monomers are only marginally stable with respect to the unfolded state, and the dimerization reaction provides a modest driving force at micromolar concentrations of protein. Mutations can readily shift the equilibrium from the dimeric native state towards weakly folded states that have a lower affinity for inhibitors but that could be induced to bind to their target proteolytic sites. Subsequent secondary mutations may increase the stability of the native dimeric state in these variants and, thereby, optimize the catalytic properties of the resistant human immunodeficiency virus type 1 protease	Human immunodeficiency virus 1

Renatured (Comment)

Organism

determination of folding free-energy surface of a pseudo-wild-type variant, by a combination of equilibrium and kinetic experiments on the urea-induced unfolding/refolding reactions. Data reveal the presence of a fully folded monomeric intermediate that associates to form the native dimeric structure, with the presence of a transient intermediate in the monomer folding reaction. The partially folded and fully folded monomers are only marginally stable with respect to the unfolded state, and the dimerization reaction provides a modest driving force at micromolar concentrations of protein. Mutations can readily shift the equilibrium from the dimeric native state towards weakly folded states that have a lower affinity for inhibitors but that could be induced to bind to their target proteolytic sites. Subsequent secondary mutations may increase the stability of the native dimeric state in these variants and, thereby, optimize the catalytic properties of the resistant human immunodeficiency virus type 1 protease

Human immunodeficiency virus 1

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Release 2023.1 (January 2023)