Published June 2003
| Version v1
Journal article
Direct measurement of the 15N CSA/dipolar relaxation interference from coupled HSQC spectra
- 1. University of Maryland, Department of Chemistry and Biochemistry, Center of Biomolecular Structure and Organization (United States)
- 2. Lerner Research Institute, Cleveland Clinic Foundation, Department of Molecular Biology, Center for Structural Biology (United States)
Description
Here we propose a method for the measurement of the 15N CSA/dipolar relaxation interference based on direct comparison of the 15N doublet components observed in a 1H-coupled 1H-15N HSQC-type spectrum. This allows the determination of the cross-correlation rates with no need for correction factors associated with other methods. The signal overlap problem of coupled HSQC spectra is addressed here by using the IPAP scheme (Ottiger et al., 1998). The approach is applied to the B3 domain of protein G to show that the method provides accurate measurements of the 15N CSA/dipolar cross-correlation rates
Additional details
Identifiers
Publishing Information
- Journal Title
- Journal of Biomolecular NMR
- Journal Volume
- 26
- Journal Issue
- 2
- Journal Page Range
- p. 181-186
- ISSN
- 0925-2738
INIS
- Country of Publication
- Netherlands
- Country of Input or Organization
- International Atomic Energy Agency (IAEA)
- INIS RN
- 39109546
- Subject category
- S60: APPLIED LIFE SCIENCES;
- Descriptors DEI
- HYDROGEN 1; NITROGEN 15; PROTEIN STRUCTURE; PROTEINS; RELAXATION; SPECTRA
- Descriptors DEC
- HYDROGEN ISOTOPES; ISOTOPES; LIGHT NUCLEI; NITROGEN ISOTOPES; NUCLEI; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; STABLE ISOTOPES
Optional Information
- Copyright
- Copyright (c) 2003 Kluwer Academic Publishers