通过固态核磁共振光谱法研究晶体蛋白中位点特异性主链动力学。

Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy.

作者信息

Giraud Nicolas, Böckmann Anja, Lesage Anne, Penin François, Blackledge Martin, Emsley Lyndon

机构信息

Laboratoire de Chimie, UMR 5182 CNRS/ENS, Laboratoire de Recherche Conventionné du CEA (no. 23V), Ecole Normale Supérieure de Lyon, 69364 Lyon, France.

出版信息

J Am Chem Soc. 2004 Sep 22;126(37):11422-3. doi: 10.1021/ja046578g.

DOI:10.1021/ja046578g

PMID:15366872

Abstract

Site-specific nitrogen-15 longitudinal relaxation rates are measured for the microcrystalline dimeric form of the protein Crh using multidimensional high-resolution solid-state NMR methods. The measured rates are used to provide a qualitative description of the site-specific internal mobility of the protein present in the solid state.

摘要

使用多维高分辨率固态核磁共振方法测量了蛋白质Crh微晶二聚体形式的位点特异性氮-15纵向弛豫率。所测量的弛豫率用于定性描述固态中蛋白质的位点特异性内部流动性。