| pubmed-article:10433696 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10433696 | lifeskim:mentions | umls-concept:C0327441 | lld:lifeskim |
| pubmed-article:10433696 | lifeskim:mentions | umls-concept:C0012590 | lld:lifeskim |
| pubmed-article:10433696 | lifeskim:mentions | umls-concept:C1956032 | lld:lifeskim |
| pubmed-article:10433696 | lifeskim:mentions | umls-concept:C1261322 | lld:lifeskim |
| pubmed-article:10433696 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
| pubmed-article:10433696 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:10433696 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:10433696 | lifeskim:mentions | umls-concept:C0678640 | lld:lifeskim |
| pubmed-article:10433696 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
| pubmed-article:10433696 | pubmed:issue | 31 | lld:pubmed |
| pubmed-article:10433696 | pubmed:dateCreated | 1999-9-3 | lld:pubmed |
| pubmed-article:10433696 | pubmed:abstractText | The conformational stability of a small ( approximately 7 kDa), all beta-sheet protein, cardiotoxin analogue III (CTX III), from the venom of the Taiwan cobra has been investigated by hydrogen-deuterium (H/D) exchange using two-dimensional NMR spectroscopy. The H/D exchange kinetics of backbone amide protons in CTX III has been monitored at pD 3.6 and 6.6 (at 25 degrees C), for over 5000 h. Examination of H/D exchange kinetics in the protein showed that a number of slowly exchanging residues are in the hydrophobic core of the protein. The average protection factor of the amide protons of residues belonging to the triple-stranded beta-sheet domain is about 20 times greater than that of those in the double-stranded beta-sheet segment. The residues in the C-terminal tail of the molecule, though structureless, have been found to exhibit significant protection against H/D exchange. Comparison of the quenched-flow H/D exchange data on CTX III with those obtained in the present study reveals that the most slowly exchanging portion constitutes the folding core of the protein. | lld:pubmed |
| pubmed-article:10433696 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10433696 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10433696 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10433696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10433696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10433696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10433696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10433696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10433696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10433696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10433696 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10433696 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:10433696 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:10433696 | pubmed:author | pubmed-author:YoII | lld:pubmed |
| pubmed-article:10433696 | pubmed:author | pubmed-author:KumarT KTK | lld:pubmed |
| pubmed-article:10433696 | pubmed:author | pubmed-author:SivaramanTT | lld:pubmed |
| pubmed-article:10433696 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10433696 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:10433696 | pubmed:volume | 38 | lld:pubmed |
| pubmed-article:10433696 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10433696 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10433696 | pubmed:pagination | 9899-905 | lld:pubmed |
| pubmed-article:10433696 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:10433696 | pubmed:meshHeading | pubmed-meshheading:10433696... | lld:pubmed |
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| pubmed-article:10433696 | pubmed:meshHeading | pubmed-meshheading:10433696... | lld:pubmed |
| pubmed-article:10433696 | pubmed:meshHeading | pubmed-meshheading:10433696... | lld:pubmed |
| pubmed-article:10433696 | pubmed:meshHeading | pubmed-meshheading:10433696... | lld:pubmed |
| pubmed-article:10433696 | pubmed:meshHeading | pubmed-meshheading:10433696... | lld:pubmed |
| pubmed-article:10433696 | pubmed:meshHeading | pubmed-meshheading:10433696... | lld:pubmed |
| pubmed-article:10433696 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10433696 | pubmed:articleTitle | Investigation of the structural stability of cardiotoxin analogue III from the Taiwan cobra by hydrogen-deuterium exchange kinetics. | lld:pubmed |
| pubmed-article:10433696 | pubmed:affiliation | Department of Chemistry, National Tsing Hua University, Hsinchu, Taiwan. | lld:pubmed |
| pubmed-article:10433696 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10433696 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10433696 | lld:pubmed |
