GFT projection NMR for efficient 1H/13C sugar spin system identification in nucleic acids

被引：5

作者：

Atreya, Hanudatta S. ^{[2
]}

Sathyamoorthy, Bharathwaj ^{[1
]}

Jaipuria, Garima ^{[2
]}

Beaumont, Victor ^{[1
]}

Varani, Gabriele ^{[3
,4
]}

Szyperski, Thomas ^{[1
]}

机构：

[1] SUNY Buffalo, Dept Chem, Buffalo, NY 14260 USA

[2] Indian Inst Sci, NMR Res Ctr, Bangalore 560012, Karnataka, India

[3] Univ Washington, Dept Chem, Seattle, WA 98195 USA

[4] Univ Washington, Dept Biochem, Seattle, WA 98195 USA

来源：

JOURNAL OF BIOMOLECULAR NMR | 2012年 / 54卷 / 04期

基金：

美国国家科学基金会;

关键词：

GFT projection NMR; Nucleic acids; Resonance assignment; RNA; DIFFERENCE CONSTANT-TIME; J-COUPLING-CONSTANTS; C-13; N-15-LABELED DNA; SCALAR COUPLINGS; RNA; SPECTROSCOPY; ASSIGNMENT; PROTEINS; DYNAMICS;

D O I：

10.1007/s10858-012-9687-5

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：

A newly implemented G-matrix Fourier transform (GFT) (4,3)D HC(C)CH experiment is presented in conjunction with (4,3)D HCCH to efficiently identify H-1/C-13 sugar spin systems in C-13 labeled nucleic acids. This experiment enables rapid collection of highly resolved relay 4D HC(C)CH spectral information, that is, shift correlations of C-13-H-1 groups separated by two carbon bonds. For RNA, (4,3)D HC(C)CH takes advantage of the comparably favorable 1'- and 3'-CH signal dispersion for complete spin system identification including 5'-CH. The (4,3)D HC(C)CH/HCCH based strategy is exemplified for the 30-nucleotide 3'-untranslated region of the pre-mRNA of human U1A protein.

引用

页码：337 / 342

页数：6

共 46 条

[1] Rapid NMR data collection [J].

Atreya, HS ;

Szyperski, T .

NUCLEAR MAGNETIC RESONANCE OF BIOLOGICAL MACROMOLECULES, PART C, 2005, 394 :78-108

[2] Resonance assignment of proteins with high shift degeneracy based on 5D spectral information encoded in G2FT NMR experiments [J].

Atreya, HS ;

Eletsky, A ;

Szyperski, T .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (13) :4554-4555

[3] G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment [J].

Atreya, HS ;

Szyperski, T .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (26) :9642-9647

[4] THE PROGRAM XEASY FOR COMPUTER-SUPPORTED NMR SPECTRAL-ANALYSIS OF BIOLOGICAL MACROMOLECULES [J].

BARTELS, C ;

XIA, TH ;

BILLETER, M ;

GUNTERT, P ;

WUTHRICH, K .

JOURNAL OF BIOMOLECULAR NMR, 1995, 6 (01) :1-10

[5]

Batey RT, 1995, METHOD ENZYMOL, V261, P300

[6] PREPARATION OF ISOTOPICALLY LABELED RIBONUCLEOTIDES FOR MULTIDIMENSIONAL NMR-SPECTROSCOPY OF RNA [J].

BATEY, RT ;

INADA, M ;

KUJAWINSKI, E ;

PUGLISI, JD ;

WILLIAMSON, JR .

NUCLEIC ACIDS RESEARCH, 1992, 20 (17) :4515-4523

[7] Refinement of the structure of protein-RNA complexes by residual dipolar coupling analysis [J].

Bayer, P ;

Varani, L ;

Varani, G .

JOURNAL OF BIOMOLECULAR NMR, 1999, 14 (02) :149-155

[8]

Cavanagh J, 2007, PROTEIN NMR SPECTROSCOPY: PRINCIPLES AND PRACTICE, 2ND EDITION, P1

[9] NMRPIPE - A MULTIDIMENSIONAL SPECTRAL PROCESSING SYSTEM BASED ON UNIX PIPES [J].

DELAGLIO, F ;

GRZESIEK, S ;

VUISTER, GW ;

ZHU, G ;

PFEIFER, J ;

BAX, A .

JOURNAL OF BIOMOLECULAR NMR, 1995, 6 (03) :277-293

[10] Probing structure and functional dynamics of (large) proteins with aromatic rings: L-GFT-TROSY (4,3)D HCCHNMR spectroscopy [J].

Eletsky, A ;

Atreya, HS ;

Liu, GH ;

Szyperski, T .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (42) :14578-14579

← 1 2 3 4 5 →