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Flanking aromatic residue competition influences transmembrane peptide helix dynamics
FEBS Letters ( IF 3.0 ) Pub Date : 2020-09-24 , DOI: 10.1002/1873-3468.13926
Matthew J McKay 1 , Denise V Greathouse 1 , Roger E Koeppe 1
Affiliation  

To address biophysical principles and lipid interactions that underlie the properties of membrane proteins, modifications that vary the neighbors of tryptophan residues in the highly dynamic transmembrane helix of GW4,20ALP23 (acetyl‐GGAW4A(LA)6LAW20AGA‐amide) were examined using deuterium NMR spectroscopy. It was found that L5,19GW4,20ALP23, a sequence isomer of the low to moderately dynamic GW5,19ALP23, remains highly dynamic. By contrast, a removal of W4 to produce F4,5GW20ALP23 restores a low level of dynamic averaging, similar to that of the F4,5GW19ALP23 helix. Interestingly, a high level of dynamic averaging requires the presence of both tryptophan residues W4 and W20, on opposite faces of the helix, and does not depend on whether residue 5 is Leu or Ala. Aspects of helix unwinding and potential oligomerization are discussed with respect to helix dynamic averaging and the locations of particular residues at a phosphocholine membrane interface.

中文翻译:

侧翼芳香残基竞争影响跨膜肽螺旋动力学

为了解决作为膜蛋白特性基础的生物物理原理和脂质相互作用,使用氘核磁共振波谱检查了改变 GW4,20ALP23(乙酰-GGAW4A(LA)6LAW20AGA-酰胺)高动态跨膜螺旋中色氨酸残基邻居的修饰. 发现 L5,19GW4,20ALP23,低到中等动态 GW5,19ALP23 的序列异构体,保持高度动态。相比之下,去除 W4 以产生 F4,5GW20ALP23 恢复了低水平的动态平均,类似于 F4,5GW19ALP23 螺旋。有趣的是,高水平的动态平均需要在螺旋的相对面上同时存在色氨酸残基 W4 和 W20,并且不依赖于残基 5 是 Leu 还是 Ala。
更新日期:2020-09-24
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