Macholl, S. ; Sack, I. ; Limbach, H. H. ; Pauli, J. ; Kelly, M. ; Buntkowsky, G. (2000)
Solid-state NMR study of the SH3 domain of alpha-spectrin: application of C-13-N-15 TEDOR and REDOR.
In: Magnetic Resonance in Chemistry, 38 (7)
Artikel, Bibliographie
Kurzbeschreibung (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.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2000 |
| Autor(en): | Macholl, S. ; Sack, I. ; Limbach, H. H. ; Pauli, J. ; Kelly, M. ; Buntkowsky, G. |
| Art des Eintrags: | Bibliographie |
| Titel: | Solid-state NMR study of the SH3 domain of alpha-spectrin: application of C-13-N-15 TEDOR and REDOR |
| Sprache: | Englisch |
| Publikationsjahr: | 2000 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Magnetic Resonance in Chemistry |
| Jahrgang/Volume einer Zeitschrift: | 38 |
| (Heft-)Nummer: | 7 |
| URL / URN: | http://apps.webofknowledge.com/full_record.do?product=WOS&se... |
| Kurzbeschreibung (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. |
| Freie Schlagworte: | 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 |
| Zusätzliche Informationen: | 330UW Times Cited:9 Cited References Count:51 |
| Fachbereich(e)/-gebiet(e): | 07 Fachbereich Chemie 07 Fachbereich Chemie > Eduard Zintl-Institut > Fachgebiet Physikalische Chemie |
| Hinterlegungsdatum: | 27 Okt 2014 20:46 |
| Letzte Änderung: | 29 Mai 2019 10:23 |
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