使用特异性和广泛氘化的脂质和 ¹³C-²H 旋转回波双共振固态 NMR 对肽和蛋白质进行残基特异性膜定位。
Residue-specific membrane location of peptides and proteins using specifically and extensively deuterated lipids and ¹³C-²H rotational-echo double-resonance solid-state NMR.
机构信息
Department of Chemistry, Michigan State University, 578 S. Shaw Lane, East Lansing, MI 48824, USA.
出版信息
J Biomol NMR. 2013 Jan;55(1):11-7. doi: 10.1007/s10858-012-9692-8. Epub 2012 Dec 8.
Abstract
Residue-specific location of peptides in the hydrophobic core of membranes was examined using (13)C-(2)H REDOR and samples in which the lipids were selectively deuterated. The transmembrane topology of the KALP peptide was validated with this approach with substantial dephasing observed for deuteration in the bilayer center and reduced or no dephasing for deuteration closer to the headgroups. Insertion of β sheet HIV and helical and β sheet influenza virus fusion peptides into the hydrophobic core of the membrane was validated in samples with extensively deuterated lipids.
摘要
使用 (13)C-(2)H REDOR 并对脂质进行选择性氘化的方法，研究了肽在膜疏水核心中的残基特异性定位。通过这种方法验证了 KALP 肽的跨膜拓扑结构，在双层中心的氘化观察到大量去相位，而靠近头部的氘化则减少或没有去相位。在脂质广泛氘化的样品中，验证了 HIV 的β 片层和螺旋及β 片层流感病毒融合肽插入膜疏水核心。
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