Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1998-11-16
|
| pubmed:abstractText |
The effect of deuteration on the measurement of HN-HN distances in moderately sized (15 kDa) proteins is discussed. Data are presented for a 15 kDa protein which is 95% deuterated on the Halpha position, and partially (70%) deuterated at other aliphatic sites. Deuteration of the protein increases the signal intensity of HN-HN cross peaks in NOESY spectra such that dipolar couplings between protons 4-5 A apart are readily detected. Experimental data and computer simulations show that either perdeuteration or partial deuteration of the protein increases the accuracy of amide-amide distance constraints. Thus, partial deuteration can be used to obtain more accurate long-range distance constraints for structure determination by NMR.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
1090-7807
|
| pubmed:author | |
| pubmed:copyrightInfo |
Copyright 1998 Academic Press.
|
| pubmed:issnType |
Print
|
| pubmed:volume |
134
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
52-6
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading | |
| pubmed:year |
1998
|
| pubmed:articleTitle |
Effect of deuteration on the accuracy of HN-HN distance constraints.
|
| pubmed:affiliation |
Department of Biological Sciences, Carnegie Mellon University, 4400 Fifth Avenue, Pittsburgh, Pennsylvania, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|