| pubmed-article:7558589 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7558589 | lifeskim:mentions | umls-concept:C0004927 | lld:lifeskim |
| pubmed-article:7558589 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
| pubmed-article:7558589 | lifeskim:mentions | umls-concept:C0078238 | lld:lifeskim |
| pubmed-article:7558589 | lifeskim:mentions | umls-concept:C0024485 | lld:lifeskim |
| pubmed-article:7558589 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:7558589 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:7558589 | lifeskim:mentions | umls-concept:C0597551 | lld:lifeskim |
| pubmed-article:7558589 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:7558589 | pubmed:dateCreated | 1995-11-6 | lld:pubmed |
| pubmed-article:7558589 | pubmed:abstractText | The solution structure of a synthetic 22-amino acid peptide (P1) corresponding to the extreme C-terminal end and one of the F-actin binding sites of villin has been determined by 1H NMR and CD spectroscopy. The structure of this peptide was compared to that of a peptide in which lysine to glutamic acid substitutions were introduced at positions 17 and 19 (P11), abolishing F-actin binding. Both peptides are largely unstructured in aqueous solution. Changes observed in the NMR and CD spectra of both peptides are consistent with alpha-helix formation in trifluoroethanol/water mixtures. A set of 189 interproton distances derived from nuclear Overhauser enhancement (NOE) measurements, 17 phi-angle constraints obtained from 3JNH alpha coupling constants, as well as about 10 N ... O distance restraints deduced from amide proton exchange kinetics with deuterium, were used for the structure determination. The three-dimensional structure of P1 and P11 is characterized by two helical regions, one extending from residues 2 to 5 and a second covering residues 7 to 17. The central fragment, ranging from Leu-7 to Leu-15, is more stable. The C-terminal residues are less structured, particularly within peptide P11. The significance of these structural results is discussed in relation to the biological activity of villin. | lld:pubmed |
| pubmed-article:7558589 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7558589 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7558589 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7558589 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7558589 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7558589 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7558589 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7558589 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7558589 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7558589 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7558589 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:7558589 | pubmed:issn | 0367-8377 | lld:pubmed |
| pubmed-article:7558589 | pubmed:author | pubmed-author:GoethalsMM | lld:pubmed |
| pubmed-article:7558589 | pubmed:author | pubmed-author:LouvardDD | lld:pubmed |
| pubmed-article:7558589 | pubmed:author | pubmed-author:Vandekerckhov... | lld:pubmed |
| pubmed-article:7558589 | pubmed:author | pubmed-author:RoseTT | lld:pubmed |
| pubmed-article:7558589 | pubmed:author | pubmed-author:FriederichEE | lld:pubmed |
| pubmed-article:7558589 | pubmed:author | pubmed-author:DelepierreMM | lld:pubmed |
| pubmed-article:7558589 | pubmed:author | pubmed-author:SimenelCC | lld:pubmed |
| pubmed-article:7558589 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7558589 | pubmed:volume | 45 | lld:pubmed |
| pubmed-article:7558589 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7558589 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7558589 | pubmed:pagination | 574-86 | lld:pubmed |
| pubmed-article:7558589 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:7558589 | pubmed:meshHeading | pubmed-meshheading:7558589-... | lld:pubmed |
| pubmed-article:7558589 | pubmed:meshHeading | pubmed-meshheading:7558589-... | lld:pubmed |
| pubmed-article:7558589 | pubmed:meshHeading | pubmed-meshheading:7558589-... | lld:pubmed |
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| pubmed-article:7558589 | pubmed:meshHeading | pubmed-meshheading:7558589-... | lld:pubmed |
| pubmed-article:7558589 | pubmed:meshHeading | pubmed-meshheading:7558589-... | lld:pubmed |
| pubmed-article:7558589 | pubmed:meshHeading | pubmed-meshheading:7558589-... | lld:pubmed |
| pubmed-article:7558589 | pubmed:meshHeading | pubmed-meshheading:7558589-... | lld:pubmed |
| pubmed-article:7558589 | pubmed:meshHeading | pubmed-meshheading:7558589-... | lld:pubmed |
| pubmed-article:7558589 | pubmed:meshHeading | pubmed-meshheading:7558589-... | lld:pubmed |
| pubmed-article:7558589 | pubmed:meshHeading | pubmed-meshheading:7558589-... | lld:pubmed |
| pubmed-article:7558589 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7558589 | pubmed:articleTitle | Conformational behaviour of a synthetic peptide of the C-terminus of villin that interacts with actin: an NMR, CD and stimulated annealing study. | lld:pubmed |
| pubmed-article:7558589 | pubmed:affiliation | NMR Laboratory, Pasteur Institute, CNRS URA 1129, Paris, France. | lld:pubmed |
| pubmed-article:7558589 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7558589 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7558589 | lld:pubmed |
