| pubmed-article:10382309 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:10382309 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:10382309 | lifeskim:mentions | umls-concept:C0680730 | lld:lifeskim |
| pubmed-article:10382309 | lifeskim:mentions | umls-concept:C0024485 | lld:lifeskim |
| pubmed-article:10382309 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:10382309 | lifeskim:mentions | umls-concept:C0185125 | lld:lifeskim |
| pubmed-article:10382309 | lifeskim:mentions | umls-concept:C1148554 | lld:lifeskim |
| pubmed-article:10382309 | lifeskim:mentions | umls-concept:C1706907 | lld:lifeskim |
| pubmed-article:10382309 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10382309 | pubmed:dateCreated | 1999-7-22 | lld:pubmed |
| pubmed-article:10382309 | pubmed:abstractText | NMR investigations of larger macromolecules (> 20 kDa) are severely hindered by rapid 1H and 13C transverse relaxation. Replacement of non-exchangeable protons with deuterium removes many efficient 1H-1H and 1H-13C relaxation pathways. The main disadvantage of deuteration is that many of the protons which would normally be the source of NOE-based distance restraints are removed. We report the development of a novel labeling strategy which is based on specific protonation and 14N-labeling of the residues phenylalanine, tyrosine, threonine, isoleucine and valine in a fully deuterated, 15N-labeled background. This allows the application of heteronuclear half-filters, 15N-editing and 1H-TOCSY experiments to select for particular magnetization transfer pathways. Results from investigations of a 47 kDa dimeric protein labeled in this way demonstrated that the method provides useful information for the structure determination of large proteins. | lld:pubmed |
| pubmed-article:10382309 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10382309 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10382309 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10382309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10382309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10382309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10382309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10382309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10382309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10382309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10382309 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10382309 | pubmed:month | May | lld:pubmed |
| pubmed-article:10382309 | pubmed:issn | 0925-2738 | lld:pubmed |
| pubmed-article:10382309 | pubmed:author | pubmed-author:KellyM JMJ | lld:pubmed |
| pubmed-article:10382309 | pubmed:author | pubmed-author:RichterGG | lld:pubmed |
| pubmed-article:10382309 | pubmed:author | pubmed-author:BacherAA | lld:pubmed |
| pubmed-article:10382309 | pubmed:author | pubmed-author:YoSS | lld:pubmed |
| pubmed-article:10382309 | pubmed:author | pubmed-author:KriegelYY | lld:pubmed |
| pubmed-article:10382309 | pubmed:author | pubmed-author:SchmiederPP | lld:pubmed |
| pubmed-article:10382309 | pubmed:author | pubmed-author:OschkinatHH | lld:pubmed |
| pubmed-article:10382309 | pubmed:author | pubmed-author:BallL JLJ | lld:pubmed |
| pubmed-article:10382309 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10382309 | pubmed:volume | 14 | lld:pubmed |
| pubmed-article:10382309 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10382309 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10382309 | pubmed:pagination | 79-83 | lld:pubmed |
| pubmed-article:10382309 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10382309 | pubmed:meshHeading | pubmed-meshheading:10382309... | lld:pubmed |
| pubmed-article:10382309 | pubmed:meshHeading | pubmed-meshheading:10382309... | lld:pubmed |
| pubmed-article:10382309 | pubmed:meshHeading | pubmed-meshheading:10382309... | lld:pubmed |
| pubmed-article:10382309 | pubmed:meshHeading | pubmed-meshheading:10382309... | lld:pubmed |
| pubmed-article:10382309 | pubmed:meshHeading | pubmed-meshheading:10382309... | lld:pubmed |
| pubmed-article:10382309 | pubmed:meshHeading | pubmed-meshheading:10382309... | lld:pubmed |
| pubmed-article:10382309 | pubmed:meshHeading | pubmed-meshheading:10382309... | lld:pubmed |
| pubmed-article:10382309 | pubmed:meshHeading | pubmed-meshheading:10382309... | lld:pubmed |
| pubmed-article:10382309 | pubmed:meshHeading | pubmed-meshheading:10382309... | lld:pubmed |
| pubmed-article:10382309 | pubmed:meshHeading | pubmed-meshheading:10382309... | lld:pubmed |
| pubmed-article:10382309 | pubmed:meshHeading | pubmed-meshheading:10382309... | lld:pubmed |
| pubmed-article:10382309 | pubmed:meshHeading | pubmed-meshheading:10382309... | lld:pubmed |
| pubmed-article:10382309 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10382309 | pubmed:articleTitle | Application of amino acid type-specific 1H- and 14N-labeling in a 2H-, 15N-labeled background to a 47 kDa homodimer: potential for NMR structure determination of large proteins. | lld:pubmed |
| pubmed-article:10382309 | pubmed:affiliation | Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany. kelly@fmp-berlin.de | lld:pubmed |
| pubmed-article:10382309 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10382309 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10382309 | lld:pubmed |
