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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1995-5-10
|
| pubmed:abstractText |
A pulsed-field gradient-enhanced, heteronuclear cross-polarization-driven, 3D HCCH-TOCSY experiment is described, which in a single scan can achieve nearly ideal solvent suppression for protein samples in H2O solution. The 3D experiment can be transformed without additional pre- or post-processing, thus leaving solute resonances at the solvent resonance position undisturbed and easily identifiable. As the gradients are used in combination with a 13C z-filter, only minimal relaxation losses are encountered as compared to non-gradient versions.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0925-2738
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
5
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
207-11
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading | |
| pubmed:year |
1995
|
| pubmed:articleTitle |
HCCH-TOCSY spectroscopy of 13C-labeled proteins in H2O using heteronuclear cross-polarization and pulsed-field gradients.
|
| pubmed:affiliation |
Biophysics Research Division, University of Michigan, Ann Arbor 48109-1055.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|