Probing secondary, tertiary, and quaternary structure along with protein-cofactor interactions for a helical transmembrane protein complex through 1H spin diffusion with MAS NMR spectroscopy

被引:13
作者
Ganapathy, Swapna [1 ]
van Gammeren, Adriaan J. [1 ]
Hulsbergen, Frans B. [1 ]
de Groot, Huub J. M. [1 ]
机构
[1] Leiden Univ, Gorlaeus Labs, Leiden Inst Chem, NL-2300 RA Leiden, Netherlands
关键词
D O I
10.1021/ja0664436
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Structure determination of membrane proteins with magic angle spinning NMR is rapidly developing. Probing secondary, tertiary, and quaternary structure along with protein-cofactor interactions through H-1 spin diffusion with MAS NMR is demonstrated for a helical transmembrane model protein complex.
引用
收藏
页码:1504 / +
页数:3
相关论文
共 28 条
[1]   Solid state NMR sequential resonance assignments and conformational analysis of the 2 x 10.4 kDa dimeric form of the Bacillus subtilis protein Crh [J].
Böckmann, A ;
Lange, A ;
Galinier, A ;
Luca, S ;
Giraud, N ;
Juy, M ;
Heise, H ;
Montserret, R ;
Penin, F ;
Baldus, M .
JOURNAL OF BIOMOLECULAR NMR, 2003, 27 (04) :323-339
[2]   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
[3]   1H and 13C MAS NMR evidence for pronounced ligand-protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin [J].
Creemers, AFL ;
Kiihne, S ;
Bovee-Geurts, PHM ;
DeGrip, WJ ;
Lugtenburg, J ;
de Groot, HJM .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (14) :9101-9106
[4]   MAS NMR structure of a microcrystalline Cd-bacteriochlorophyll d analogue [J].
de Boer, I ;
Matysik, J ;
Amakawa, M ;
Yagai, S ;
Tamiaki, H ;
Holzwarth, AR ;
de Groot, HJM .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2003, 125 (44) :13374-13375
[5]   2D13C-13C MAS NMR correlation spectroscopy with mixing by true 1H spin diffusion reveals long-range intermolecular distance restraints in ultra high magnetic field [J].
de Boer, I ;
Bosman, L ;
Raap, J ;
Oschkinat, H ;
de Groot, HJM .
JOURNAL OF MAGNETIC RESONANCE, 2002, 157 (02) :286-291
[6]   Magic-angle spinning solid-state NMR spectroscopy of the β1 immunoglobulin binding domain of protein G (GB1):: 15N and 13C chemical shift assignments and conformational analysis [J].
Franks, WT ;
Zhou, DH ;
Wylie, BJ ;
Money, BG ;
Graesser, DT ;
Frericks, HL ;
Sahota, G ;
Rienstra, CM .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (35) :12291-12305
[7]   Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR [J].
Heise, H ;
Hoyer, W ;
Becker, S ;
Andronesi, OC ;
Riedel, D ;
Baldus, M .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (44) :15871-15876
[8]   Assignments of carbon NMR resonances for microcrystalline ubiquitin [J].
Igumenova, TI ;
McDermott, AE ;
Zilm, KW ;
Martin, RW ;
Paulson, EK ;
Wand, AJ .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2004, 126 (21) :6720-6727
[9]   Assignment of the backbone resonances for microcrystalline ubiquitin [J].
Igumenova, TI ;
Wand, AJ ;
McDermott, AE .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2004, 126 (16) :5323-5331
[10]   High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy [J].
Jaroniec, CP ;
MacPhee, CE ;
Bajaj, VS ;
McMahon, MT ;
Dobson, CM ;
Griffin, RG .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (03) :711-716