title: Use of thiol-disulfide exchange method to study transmembrane peptide association in membrane environments.
abstract: The development of methods for reversibly folding membrane proteins in a two-state manner remains a considerable challenge for studies of membrane protein stability. In recent years, a variety of techniques have been established and studies of membrane protein folding thermodynamics in the native bilayer environments have become feasible. Here we present the thiol-disulfide exchange method, a promising experimental approach for investigating the thermodynamics of transmembrane (TM) helix-helix association in membrane-mimicking environments. The method involves initiating disulfide cross-linking of a protein under reversible redox conditions in a thiol-disulfide buffer and quantitative assessment of the extent of cross-linking at equilibrium. This experimental method provides a broadly applicable tool for thermodynamic studies of folding, oligomerization, and helix-helix interactions of membrane proteins.
authors: Influmedix, Inc., Radnor, PA, USA.
authors: Lidia
authors: L
authors: Cristian
authors: Yao
authors: Y
authors: Zhang
mesh_terms: D002462:Cell Membrane / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D056148:Chromatography, Reverse-Phase; D003902:Detergents / Q000737:chemistry; D004220:Disulfides / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D010084:Oxidation-Reduction; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D025941:Protein Interaction Mapping / Q000379:methods*; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D013438:Sulfhydryl Compounds / Q000737:chemistry*
chemical_list: D003902:Detergents; D004220:Disulfides; D008565:Membrane Proteins; D010455:Peptides; D013438:Sulfhydryl Compounds