| pubmed-article:10024451 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10024451 | lifeskim:mentions | umls-concept:C0206394 | lld:lifeskim |
| pubmed-article:10024451 | lifeskim:mentions | umls-concept:C0206397 | lld:lifeskim |
| pubmed-article:10024451 | lifeskim:mentions | umls-concept:C1623051 | lld:lifeskim |
| pubmed-article:10024451 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:10024451 | lifeskim:mentions | umls-concept:C1136102 | lld:lifeskim |
| pubmed-article:10024451 | lifeskim:mentions | umls-concept:C0039476 | lld:lifeskim |
| pubmed-article:10024451 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:10024451 | lifeskim:mentions | umls-concept:C0019409 | lld:lifeskim |
| pubmed-article:10024451 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
| pubmed-article:10024451 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:10024451 | pubmed:dateCreated | 1999-4-13 | lld:pubmed |
| pubmed-article:10024451 | pubmed:abstractText | Solid-state NMR spectroscopy was used to analyze the conformational heterogeneity of the major coat protein (pVIII) of filamentous bacteriophage fd. Both one and two-dimensional solid-state NMR spectra of magnetically aligned samples of fd bacteriophage reveal that an increase in temperature and a single site substitution (Tyr21 to Met, Y21M) reduce the conformational heterogeneity observed throughout wild-type pVIII. The NMR results are consistent with previous studies indicating that conformational flexibility in the hinge-bend segment that links the amphipathic and hydrophobic helices in the membrane-bound form of the protein plays an essential role during phage assembly, which involves a major change in the tertiary, but not secondary, structure of the coat protein. | lld:pubmed |
| pubmed-article:10024451 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10024451 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10024451 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10024451 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10024451 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10024451 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10024451 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10024451 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10024451 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10024451 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:10024451 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:10024451 | pubmed:author | pubmed-author:PerhamR NRN | lld:pubmed |
| pubmed-article:10024451 | pubmed:author | pubmed-author:OpellaS JSJ | lld:pubmed |
| pubmed-article:10024451 | pubmed:author | pubmed-author:JelinekRR | lld:pubmed |
| pubmed-article:10024451 | pubmed:author | pubmed-author:MalikPP | lld:pubmed |
| pubmed-article:10024451 | pubmed:author | pubmed-author:NyeR EREJr | lld:pubmed |
| pubmed-article:10024451 | pubmed:author | pubmed-author:TerryT DTD | lld:pubmed |
| pubmed-article:10024451 | pubmed:copyrightInfo | Copyright 1999 Academic Press. | lld:pubmed |
| pubmed-article:10024451 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10024451 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:10024451 | pubmed:volume | 286 | lld:pubmed |
| pubmed-article:10024451 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10024451 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10024451 | pubmed:pagination | 787-96 | lld:pubmed |
| pubmed-article:10024451 | pubmed:dateRevised | 2009-9-29 | lld:pubmed |
| pubmed-article:10024451 | pubmed:meshHeading | pubmed-meshheading:10024451... | lld:pubmed |
| pubmed-article:10024451 | pubmed:meshHeading | pubmed-meshheading:10024451... | lld:pubmed |
| pubmed-article:10024451 | pubmed:meshHeading | pubmed-meshheading:10024451... | lld:pubmed |
| pubmed-article:10024451 | pubmed:meshHeading | pubmed-meshheading:10024451... | lld:pubmed |
| pubmed-article:10024451 | pubmed:meshHeading | pubmed-meshheading:10024451... | lld:pubmed |
| pubmed-article:10024451 | pubmed:meshHeading | pubmed-meshheading:10024451... | lld:pubmed |
| pubmed-article:10024451 | pubmed:meshHeading | pubmed-meshheading:10024451... | lld:pubmed |
| pubmed-article:10024451 | pubmed:meshHeading | pubmed-meshheading:10024451... | lld:pubmed |
| pubmed-article:10024451 | pubmed:meshHeading | pubmed-meshheading:10024451... | lld:pubmed |
| pubmed-article:10024451 | pubmed:meshHeading | pubmed-meshheading:10024451... | lld:pubmed |
| pubmed-article:10024451 | pubmed:meshHeading | pubmed-meshheading:10024451... | lld:pubmed |
| pubmed-article:10024451 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10024451 | pubmed:articleTitle | Effects of temperature and Y21M mutation on conformational heterogeneity of the major coat protein (pVIII) of filamentous bacteriophage fd. | lld:pubmed |
| pubmed-article:10024451 | pubmed:affiliation | Department of Chemistry, University of Pennsylvania, Philadelphia, PA, 19104, USA. | lld:pubmed |
| pubmed-article:10024451 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10024451 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10024451 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10024451 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10024451 | lld:pubmed |
