Journal article
Conformation of a double-membrane-spanning fragment of a G protein-coupled receptor: Effects of hydrophobic environment and pH
Abstract
Overcoming the problems associated with the expression, purification and in vitro handling of membrane proteins requires an understanding of the factors governing the folding and stability of such proteins in detergent solutions. As a sequel to our earlier report (Biochim. Biophys. Acta 1747(2005), 133-140), we describe an improved purification procedure and a detailed structural analysis of a fragment of the mu-opioid receptor ('TM2-3') that …
Authors
Kerman A; Ananthanarayanan VS
Journal
Biochimica et Biophysica Acta, Vol. 1768, No. 5, pp. 1199–1210
Publisher
Elsevier
Publication Date
5 2007
DOI
10.1016/j.bbamem.2007.01.017
ISSN
0006-3002
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Amino Acid SequenceCircular DichroismDetergentsHistidineHydrogen-Ion ConcentrationHydrophobic and Hydrophilic InteractionsMass SpectrometryMolecular Sequence DataOligopeptidesProtein Processing, Post-TranslationalProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryReceptors, Opioid, muStructural Homology, ProteinTrypsin