[摘要] 19F NMR and CD spectra reveal that bacteriorhodopsin as well as its 5-fluorotryptophan-labeled analog solubilized in a CH3OH-CHCl3 mixture (i) retains a secondary structure of the fully active chromoprotein in the purple membrane and (ii) possesses a folded structure in which modifications at the Lys-216 bound retinal are sensed by sequentially remote tryptophan residues. Individual fragments isolated after limited proteolysis and NaBH4-cleavage of bacteriorhodopsin keep the spatial structure of the intact polypeptide chain in the organic solvent.
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[效力级别] [学科分类] 生物化学/生物物理
[关键词] Bacteriorhodopsin;Membrane protein solubilization;Protein structure;19F-NMR;CD;bR;bacteriorhodopsin;bR(F);5-fluorotryptophan labeled bacteriorhodopsin;RetbO(F);5-fluorotryptophan labeled retinylbacterioopsin;Ret'bO(F);5-fluorotryptophan labeled 1;1;5-tridesmethyl-1;2;3;4-tetrahydro-3-fluororetinylbacterioopsin;C1;Gly-72-Ser-248 peptide of RetbO(F);C2;< Glu-1-Phe-71 peptide of RetbO(F);B1;< Glu-1-Gly-155 peptide of RetbO(F);B2;Phe-156-Ser-248 peptide of Retbo(F);NMR;nuclear magnetic resonance;CD;circular dichroism [时效性]
