期刊
JOURNAL OF BIOMOLECULAR NMR
卷 34, 期 1, 页码 31-40出版社
SPRINGER
DOI: 10.1007/s10858-005-5338-4
关键词
NOESY; NRPS; nuclear magnetic resonance; protein structure; time-shared
资金
- NCRR NIH HHS [RR 00995] Funding Source: Medline
- NIGMS NIH HHS [GM 47467, P01 GM047467] Funding Source: Medline
- NATIONAL CENTER FOR RESEARCH RESOURCES [P41RR000995] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P01GM047467] Funding Source: NIH RePORTER
We present two time-shared experiments that enable the characterization of all nOes in H-1-C-13-ILV methyl-labelled proteins that are otherwise uniformly deuterated and N-15 enriched and possibly selectively protonated for distinct residue types. A 3D experiment simultaneously provides the spectra of a 3D NOESY-HN-TROSY and of a 3D NOESY-HC-PEP-HSQC. Thus, nOes from any protons to methyl or amide protons are dispersed with respect to N-15 and C-13 chemical shifts, respectively. The single 4D experiment presented here yields simultaneously the four 4D experiments HC-HSQC-NOESY-HC-PEP-HSQC, HC-HSQC-NOESY-HN-TROSY, HN-HSQC-NOESY-HN-TROSY and HN-HSQC-NOESY-HC-PEP-HSQC. This allows for the unambiguous determination of all nOes involving amide and methyl protons. The method was applied to a (H-1,C-13)-ILV-(H-1)-FY-(U-H-2,N-15) sample of a 37 kDa di-domain of the E. coli enterobactin synthetase module EntF.
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