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Relaxation-compensated difference spin diffusion NMR for detecting 13C-13C long-range correlations in proteins and polysaccharides.
- Source :
-
Journal of biomolecular NMR [J Biomol NMR] 2015 Feb; Vol. 61 (2), pp. 97-107. Date of Electronic Publication: 2014 Dec 16. - Publication Year :
- 2015
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Abstract
- The measurement of long-range distances remains a challenge in solid-state NMR structure determination of biological macromolecules. In 2D and 3D correlation spectra of uniformly (13)C-labeled biomolecules, inter-residue, inter-segmental, and intermolecular (13)C-(13)C cross peaks that provide important long-range distance constraints for three-dimensional structures often overlap with short-range cross peaks that only reflect the covalent structure of the molecule. It is therefore desirable to develop new approaches to obtain spectra containing only long-range cross peaks. Here we show that a relaxation-compensated modification of the commonly used 2D (1)H-driven spin diffusion (PDSD) experiment allows the clean detection of such long-range cross peaks. By adding a z-filter to keep the total z-period of the experiment constant, we compensate for (13)C T1 relaxation. As a result, the difference spectrum between a long- and a scaled short-mixing time spectrum show only long-range correlation signals. We show that one- and two-bond cross peaks equalize within a few tens of milliseconds. Within ~200 ms, the intensity equilibrates within an amino acid residue and a monosaccharide to a value that reflects the number of spins in the local network. With T1 relaxation compensation, at longer mixing times, inter-residue and inter-segmental cross peaks increase in intensity whereas intra-segmental cross-peak intensities remain unchanged relative to each other and can all be subtracted out. Without relaxation compensation, the difference 2D spectra exhibit both negative and positive intensities due to heterogeneous T1 relaxation in most biomolecules, which can cause peak cancellation. We demonstrate this relaxation-compensated difference PDSD approach on amino acids, monosaccharides, a crystalline model peptide, a membrane-bound peptide and a plant cell wall sample. The resulting difference spectra yield clean multi-bond, inter-residue and intermolecular correlation peaks, which are often difficult to resolve in the parent 2D spectra.
- Subjects :
- Arabidopsis
Carbon Isotopes chemistry
Glucose chemistry
Glutamine chemistry
Histidine chemistry
N-Formylmethionine Leucyl-Phenylalanine chemistry
Plant Proteins analysis
Polysaccharides analysis
Carbon-13 Magnetic Resonance Spectroscopy methods
Cell Wall chemistry
Nuclear Magnetic Resonance, Biomolecular methods
Plant Proteins chemistry
Polysaccharides chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1573-5001
- Volume :
- 61
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Journal of biomolecular NMR
- Publication Type :
- Academic Journal
- Accession number :
- 25510834
- Full Text :
- https://doi.org/10.1007/s10858-014-9889-0