Investigations of the structure and dynamics of membrane-associated peptides by magic angle spinning NMR

被引：57
|
作者：
Huster, D [1 ]
机构：
[1] Univ Leipzig, Inst Med Phys & Biophys, Ctr Biotechnol & Biomed, Jr Res Grp Solid State NMR Studies Membrane Assoc, D-04107 Leipzig, Germany
来源：
PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY | 2005年 / 46卷 / 2-3期
关键词：
solid-state NMR; bilayer; polypeptides; magainin; K3; protegrin-1; glycophorin A; Ras; human calcitonin; FP23 from gp41 of HIV-1; MARCKS;
D O I：
10.1016/j.pnmrs.2005.01.001
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
The structure and dynamics of membrane-associated peptides were investigated by using magic angle spinning NMR. The interactions of peptides with is significant to understand several biological problems and helps in biotechnological applications. The short peptide sequences, synthesizes by cells are part of immune system, the metabolism of of living organisms, single transduction events, catalysis of chemical reactions and so on. With the recent technical improvements, solid-state NMR gained the highest potential to solve complete structures of membrane-associated peptides and proteins.
引用
收藏
页码：79 / 107
页数：29
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