19F NMR study of 5‐fluorotryptophan‐labeled bacteriorhodopsin

FEBS Letters

Tsetlin, V.I.¹  Ovchinnikov, Yu.A.¹  Arseniev, A.S.¹  Kuryatov, A.B.¹  Bystrov, V.F.¹  Ivanov, V.T.¹ 

[1] Shemyakin Institute of Bioorganic Chemistry, USSR Academy of Sciences, Ul. Miklukho-Maklaya 16/10, 117871 GSP Moscow, USSR

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;   

DOI  :  10.1016/0014-5793(87)81506-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown