Solid-state NMR structure determination

被引:50
作者
Drechsler, A [1 ]
Separovic, F [1 ]
机构
[1] Univ Melbourne, Sch Chem, Melbourne, Vic 3010, Australia
关键词
solid-state NMR; protein structure; membrane peptides; GRAMICIDIN-A; C-13; NMR; ORIENTATION; PROTEINS; PEPTIDE; CONFORMATION; MEMBRANES; MELITTIN; INSIGHTS; CHAIN;
D O I
10.1080/15216540310001622740
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
Biological applications of solid-state NMR (SS-NMR) have been predominantly in the area of model membrane systems. Increasingly the focus has been membrane peptides and proteins. SS-NMR is able to provide information about how the peptides or proteins interact with the lipids or other peptides/proteins in the membrane, their effect on the membrane and the location of the peptides or proteins relative to the membrane surface. Recent developments in biological SS-NMR have been made possible by improvements in labelling and NMR techniques. This review discusses aligned systems and magic angle spinning techniques, bilayers and bicelles, and measurement of chemical shift anisotropy and dipolar coupling. A number of specific experiments such as cross polarization, rotational resonance, REDOR, PISEMA, MAOSS and multidimensional experiments are described. In addition to H-2, C-13 and N-15, recent solid-sate H-1, F-19 and O-17 NMR work is discussed. Several examples of the use of SS-NMR to determine the structure of membrane peptides and proteins are given.
引用
收藏
页码:515 / 523
页数:9
相关论文
共 41 条
[1]   The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy [J].
Bechinger, B .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 1999, 1462 (1-2) :157-183
[2]   Electrostatic peptide-lipid interactions of amyloid-β peptide and pentalysine with membrane surfaces monitored by 31P MAS NMR [J].
Bonev, B ;
Watts, A ;
Bokvist, M ;
Gröbner, G .
PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 2001, 3 (14) :2904-2910
[3]   Effects of the eukaryotic pore-forming cytolysin equinatoxin II on lipid membranes and the role of sphingomyelin [J].
Bonev, BB ;
Lam, YH ;
Anderluh, G ;
Watts, A ;
Norton, RS ;
Separovic, F .
BIOPHYSICAL JOURNAL, 2003, 84 (04) :2382-2392
[4]   Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy [J].
Castellani, F ;
van Rossum, B ;
Diehl, A ;
Schubert, M ;
Rehbein, K ;
Oschkinat, H .
NATURE, 2002, 420 (6911) :98-102
[5]   THE LOWER LIMIT TO THE SIZE OF SMALL SONICATED PHOSPHOLIPID-VESICLES [J].
CORNELL, BA ;
FLETCHER, GC ;
MIDDLEHURST, J ;
SEPAROVIC, F .
BIOCHIMICA ET BIOPHYSICA ACTA, 1982, 690 (01) :15-19
[6]   CONFORMATION AND ORIENTATION OF GRAMICIDIN-A IN ORIENTED PHOSPHOLIPID-BILAYERS MEASURED BY SOLID-STATE C-13 NMR [J].
CORNELL, BA ;
SEPAROVIC, F ;
BALDASSI, AJ ;
SMITH, R .
BIOPHYSICAL JOURNAL, 1988, 53 (01) :67-76
[7]   MAGIC-ANGLE-SPINNING C-13 NMR WITH ATOMIC RESOLUTION OF A PHOTOSYNTHETIC REACTION CENTER ENRICHED IN [4'-C-13]TYROSINE [J].
DEGROOT, HJM ;
RAAP, J ;
WINKEL, C ;
HOFF, AJ ;
LUGTENBURG, J .
CHEMICAL PHYSICS LETTERS, 1990, 169 (04) :307-310
[8]  
Duer M.J., 2002, SOLID STATE NMR SPEC
[9]  
GAWRISCH K, 2001, CURRENT TOPICS MEMBR, P163
[10]   Magic angle-oriented sample spinning (MAOSS): A new approach toward biomembrane studies [J].
Glaubitz, C ;
Watts, A .
JOURNAL OF MAGNETIC RESONANCE, 1998, 130 (02) :305-316