Thermostability of the HIV gp41 Wild-Type and Loop Mutations
Abstract:The HIV and SIV gp41 ectodomains are extremely stable to chemical and thermal denaturation and the observed stability has been proposed to be an important thermodynamic driving force for gp41-mediated fusion of the viral and target cell membranes. The importance of the disulphide bond and surrounding residues within the HIV gp41 loop have been assayed by DSC studies of wild type and mutant HIV gp41. Based on the thermal transition temperature, the disulphide bond and surrounding residues do not contribute to the thermal stability of gp41 and thus do not contribute to gp41-mediated membrane fusion.
Document Type: Research Article
Affiliations: Department of Biochemistry and Molecular Genetics,University of Illinois at Chicago, Chicago, IL 60607, USA.
Publication date: May 1, 2006
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