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Advances towards resonance assignments for uniformly--13C, 15N enriched bacteriorhodopsin at 18.8 T in purple membranes.

Abstract:

Solid state NMR spectra from uniformly (13)C, (15)N enriched bacteriorhodospin (bR) purified from H. salinarium were acquired at 18.8 T using magic angle spinning methods. Isolated resonances of 2D (13)C-(13)C spectra exhibited 0.50-0.55 ppm line-widths. Several amino acid types could be assigned, and at least 12 out of 15 Ile peaks could be resolved clearly and identified based on their characteristic chemical shifts and connectivities. This study confirms that high resolution solid state NM...

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Publication status:
Published

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Publisher copy:
10.1007/s10858-008-9235-5

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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
Journal:
Journal of biomolecular NMR
Volume:
41
Issue:
1
Pages:
1-4
Publication date:
2008-05-05
DOI:
EISSN:
1573-5001
ISSN:
0925-2738
URN:
uuid:9ac72de4-bd52-48b9-b866-efccbccbcd58
Source identifiers:
99835
Local pid:
pubs:99835

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