Hydrogen exchange from the transbilayer hydrophobic peptide of glycophorin reconstituted in lipid bilayers

FEBS Letters

Sami, Malkit¹  Dempsey, Christopher¹ 

[1] Biochemistry Department, Oxford University, South Parks Road, Oxford OX1 3QU, England

关键词: Glycophorin;    Transbilayer peptide;    Amide exchange;    Membrane protein;    Reconstitution;    bR;    bacteriorhodopsin;    HPLC;    high-performance liquid chromatography;    NMR;    nuclear magnetic resonance;    PC;    phosphatidylcholine;    T(is);    (insoluble) tryptic transbilayer peptide of glycophorin;    TFA;    trifluoroacetic acid;    TFE;    trifluoroethanol;    TLC;    thin layer chromatography;   

DOI  :  10.1016/0014-5793(88)80370-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The hydrophobic transbilayer peptide of erythrocyte glycophorin has been purified following exchange of tritium into the backbone amides, and reconstituted in egg phosphatidylcholine micelles. Analysis of tritium exchange from the backbone amides of the membrane-reconstituted peptide shows that about two of the amides are virtually non-exchangeable, about 10 are slowed by factors of 10⁷ relative to free amides in unstructured water soluble peptides and the remainder of the amides (about 20) have slowing factors of less than 1000. These classes of amides are proposed to reflect the stability of the peptide with respect to hydrogen bond breaking fluctuations and the accessibility of the amides to exchange catalysts in different regions of the bilayer.

【 授权许可】

Unknown