Molecular interactions investigated by multi-dimensional solid-state NMR

被引:52
作者
Baldus, Marc [1 ]
机构
[1] Max Planck Inst Biophys Chem, Abt NMR Basierte Strukturbiol, D-37077 Gottingen, Germany
关键词
D O I
10.1016/j.sbi.2006.08.003
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Solid-state NMR (ssNMR) offers insight into the formation of protein complexes and ligand binding for a large range of molecular sizes and binding affinities. Recent instrumental and methodological progress has enabled novel possibilities for using multi-dimensional ssNMR to study molecular 3D structures and interactions in noncrystalline systems. Two-dimensional ssNMR correlation experiments were applied to study ligand binding in globular and membrane proteins and have enabled the investigation of molecular interfaces in the context of protein folding and aggregation. In lipid bilayers, a versatile set of ssNMR experiments has been developed to study molecular structure, topology and complex formation in a functional environment.
引用
收藏
页码:618 / 623
页数:6
相关论文
共 58 条
[21]   Characterization of dynamics of perdeuterated proteins by MAS solid-state NMR [J].
Hologne, M ;
Faelber, K ;
Diehl, A ;
Reif, B .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (32) :11208-11209
[22]   Investigations of the structure and dynamics of membrane-associated peptides by magic angle spinning NMR [J].
Huster, D .
PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY, 2005, 46 (2-3) :79-107
[23]   Frequency selective heteronuclear dipolar recoupling in rotating solids:: Accurate 13C-15N distance measurements in uniformly 13C,15N-labeled peptides [J].
Jaroniec, CP ;
Tounge, BA ;
Herzfeld, J ;
Griffin, RG .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2001, 123 (15) :3507-3519
[24]   Observation of ligand binding to cytochrome P450-BM-3 by means of solid-state NMR spectroscopy [J].
Jovanovic, T ;
McDermott, AE .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (40) :13816-13821
[25]   Thermal equilibrium of high- and low-spin forms of cytochrome P450BM-3: Repositioning of the substrate? [J].
Jovanovic, T ;
Farid, R ;
Friesner, RA ;
McDermott, AE .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (39) :13548-13552
[26]   Assembly of a mixture of isomeric BChl c from Chlorobium limicola as determined by intermolecular 13C-13C dipolar correlations:: Coexistence of dimer-based and pseudo-monomer-based stackings [J].
Kakitani, Yoshinori ;
Nagae, Hiroyoshi ;
Mizoguchi, Tadashi ;
Egawa, Ayako ;
Akiba, Kengo ;
Fujiwara, Toshimichi ;
Akutsu, Hideo ;
Koyama, Yasushi .
BIOCHEMISTRY, 2006, 45 (24) :7574-7585
[27]   Towards structure determination of neurotoxin II bound to nicotinic acetylcholine receptor: a solid-state NMR approach [J].
Krabben, L ;
van Rossum, BJ ;
Castellani, F ;
Bocharov, E ;
Schulga, AA ;
Arseniev, AS ;
Weise, C ;
Hucho, F ;
Oschkinata, H .
FEBS LETTERS, 2004, 564 (03) :319-324
[28]   SPECTRAL SPIN DIFFUSION IN POLYCRYSTALLINE SOLIDS UNDER MAGIC-ANGLE SPINNING [J].
KUBO, A ;
MCDOWELL, CA .
JOURNAL OF THE CHEMICAL SOCIETY-FARADAY TRANSACTIONS I, 1988, 84 :3713-3730
[29]   Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR [J].
Lange, A ;
Giller, K ;
Hornig, S ;
Martin-Eauclaire, MF ;
Pongs, O ;
Becker, S ;
Baldus, M .
NATURE, 2006, 440 (7086) :959-962
[30]   A concept for rapid protein-structure determination by solid-state NMR spectroscopy [J].
Lange, A ;
Becker, S ;
Seidel, K ;
Giller, K ;
Pongs, O ;
Baldus, M .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2005, 44 (14) :2089-2092