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Solid-state NMR study of the SH3 domain of alpha-spectrin: application of C-13-N-15 TEDOR and REDOR

Macholl, S. and Sack, I. and Limbach, H. H. and Pauli, J. and Kelly, M. and Buntkowsky, G. (2000):
Solid-state NMR study of the SH3 domain of alpha-spectrin: application of C-13-N-15 TEDOR and REDOR.
38, In: Magnetic Resonance in Chemistry, (7), pp. 596-603, [Online-Edition: http://apps.webofknowledge.com/full_record.do?product=WOS&se...],
[Article]

Abstract

A fully C-13-N-15-labeled and a selectively alanine-C-13(beta) tryptophan-N-15(ring)-labeled sample of the Src homology region 3 (SH3) domain of alpha-spectrin (chicken), a 62 residue protein, were biosynthesized and studied by solid-state cross-polarization magic angle spinning (CP/MAS) NMR,C-13-N-15 rotational echo double resonance (REDOR) and N-15-C-13 transferred echo double resonance (TEDOR) spectroscopy. In the first part of the study it is shown that spectral editing with the TEDOR sequence leads to a drastic simplification of the C-13 MAS spectrum of the fully labeled sample, allowing the resolved spectroscopy of groups of C-13 nuclei, according to their distance to neighboring N-15 nuclei. In the second part of the study the inter-residual distance between the alanine residue Ala55 and the tryptophan residue Trp42 was determined by the measurement of the dipolar coupling between Ala-C-13(beta) and Trp-N-15(ring), yielding a dipolar coupling of 48 +/- 8 Hz, which after correction for fast molecular vibrations gives a value of 53 +/- 8 Hz, corresponding to a CN distance of 3.85 +/- 0.25 Hz. The result is compared to the CN distances obtained by x-ray diffraction and liquid-state NMR. Copyright (C) 2000 John Wiley & Sons, Ltd.

Item Type: Article
Erschienen: 2000
Creators: Macholl, S. and Sack, I. and Limbach, H. H. and Pauli, J. and Kelly, M. and Buntkowsky, G.
Title: Solid-state NMR study of the SH3 domain of alpha-spectrin: application of C-13-N-15 TEDOR and REDOR
Language: English
Abstract:

A fully C-13-N-15-labeled and a selectively alanine-C-13(beta) tryptophan-N-15(ring)-labeled sample of the Src homology region 3 (SH3) domain of alpha-spectrin (chicken), a 62 residue protein, were biosynthesized and studied by solid-state cross-polarization magic angle spinning (CP/MAS) NMR,C-13-N-15 rotational echo double resonance (REDOR) and N-15-C-13 transferred echo double resonance (TEDOR) spectroscopy. In the first part of the study it is shown that spectral editing with the TEDOR sequence leads to a drastic simplification of the C-13 MAS spectrum of the fully labeled sample, allowing the resolved spectroscopy of groups of C-13 nuclei, according to their distance to neighboring N-15 nuclei. In the second part of the study the inter-residual distance between the alanine residue Ala55 and the tryptophan residue Trp42 was determined by the measurement of the dipolar coupling between Ala-C-13(beta) and Trp-N-15(ring), yielding a dipolar coupling of 48 +/- 8 Hz, which after correction for fast molecular vibrations gives a value of 53 +/- 8 Hz, corresponding to a CN distance of 3.85 +/- 0.25 Hz. The result is compared to the CN distances obtained by x-ray diffraction and liquid-state NMR. Copyright (C) 2000 John Wiley & Sons, Ltd.

Journal or Publication Title: Magnetic Resonance in Chemistry
Volume: 38
Number: 7
Uncontrolled Keywords: sh3 domain alpha-spectrin protein tedor redor spectral editing chemical editing cn distances dipolar solid-state nmr nuclear-magnetic-resonance rotating solids 5-enolpyruvylshikimate-3-phosphate synthase distance measurements protein-structure crystal-structure molecular-sieve ternary complex magic-angle spectroscopy
Divisions: 07 Department of Chemistry
07 Department of Chemistry > Physical Chemistry
Date Deposited: 27 Oct 2014 20:46
Official URL: http://apps.webofknowledge.com/full_record.do?product=WOS&se...
Additional Information:

330UW Times Cited:9 Cited References Count:51

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