在脂质双分子层中重组的血型糖蛋白跨膜疏水肽的氢交换。

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

作者信息

Sami M, Dempsey C

机构信息

Biochemistry Department, Oxford University, England.

出版信息

FEBS Lett. 1988 Nov 21;240(1-2):211-5. doi: 10.1016/0014-5793(88)80370-3.

DOI:10.1016/0014-5793(88)80370-3

PMID:3191995

Abstract

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 10(7) 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.

摘要

在将氚交换到主链酰胺中后，红细胞血型糖蛋白的疏水跨膜肽已被纯化，并重构于卵磷脂酰胆碱微团中。对膜重构肽主链酰胺的氚交换分析表明，约两个酰胺实际上不可交换，约10个酰胺相对于无结构水溶性肽中的游离酰胺，交换速度减慢了10⁷倍，其余的酰胺（约20个）的减慢因子小于1000。这些酰胺类别被认为反映了肽相对于氢键断裂波动的稳定性以及酰胺在双层不同区域中与交换催化剂的可及性。