| pubmed-article:16091587 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16091587 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:16091587 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:16091587 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:16091587 | lifeskim:mentions | umls-concept:C1441672 | lld:lifeskim |
| pubmed-article:16091587 | lifeskim:mentions | umls-concept:C0623641 | lld:lifeskim |
| pubmed-article:16091587 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:16091587 | pubmed:dateCreated | 2005-8-10 | lld:pubmed |
| pubmed-article:16091587 | pubmed:abstractText | The crystal structure of a collagen-model peptide [(Pro-Pro-Gly)(9)](3) has been determined at 1.33 A resolution. Diffraction data were collected at 100 K using synchrotron radiation, which led to the first structural study of [(Pro-Pro-Gly)(n)](3) under cryogenic conditions. The crystals belong to the P2(1) space group with cell parameters of a = 25.95, b = 26.56, c = 80.14 Angstroms and beta = 90.0 degrees. The overall molecular conformation was consistent with the left-handed 7/2-helical model with an axial repeat of 20 A for native collagen. A total of 332 water molecules were found in an asymmetric unit. Proline residues in adjacent triple-helices exhibited three types of hydrophobic interactions. Furthermore, three types of hydrogen-bonding networks mediated by water molecules were observed between adjacent triple-helices. These hydrophobic interactions and hydrogen-bonding networks occurred at intervals of 20 Angstroms along the c-axis based on the previous sub-cell structures [(Pro-Pro-Gly)(n)](3) (n = 9, 10), which were also seen in the full-cell structure of [(Pro-Pro-Gly)(10)](3). Five proline residues at the Y position in the X-Y-Gly triplet were found in a down-puckering conformation, this being inconsistent with the recently proposed propensity-based hypothesis. These proline residues were forced to adopt opposing puckering because of the prevailing hydrophobic interaction between triple-helices compared with the Pro:Pro stacking interaction within a triple-helix. | lld:pubmed |
| pubmed-article:16091587 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16091587 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16091587 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16091587 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16091587 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16091587 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16091587 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16091587 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16091587 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16091587 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:16091587 | pubmed:issn | 0021-924X | lld:pubmed |
| pubmed-article:16091587 | pubmed:author | pubmed-author:TanakaYujiY | lld:pubmed |
| pubmed-article:16091587 | pubmed:author | pubmed-author:NishinoNorika... | lld:pubmed |
| pubmed-article:16091587 | pubmed:author | pubmed-author:OkuyamaKenjiK | lld:pubmed |
| pubmed-article:16091587 | pubmed:author | pubmed-author:NoguchiKeiich... | lld:pubmed |
| pubmed-article:16091587 | pubmed:author | pubmed-author:HongoChizuruC | lld:pubmed |
| pubmed-article:16091587 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16091587 | pubmed:volume | 138 | lld:pubmed |
| pubmed-article:16091587 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16091587 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16091587 | pubmed:pagination | 135-44 | lld:pubmed |
| pubmed-article:16091587 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:16091587 | pubmed:meshHeading | pubmed-meshheading:16091587... | lld:pubmed |
| pubmed-article:16091587 | pubmed:meshHeading | pubmed-meshheading:16091587... | lld:pubmed |
| pubmed-article:16091587 | pubmed:meshHeading | pubmed-meshheading:16091587... | lld:pubmed |
| pubmed-article:16091587 | pubmed:meshHeading | pubmed-meshheading:16091587... | lld:pubmed |
| pubmed-article:16091587 | pubmed:meshHeading | pubmed-meshheading:16091587... | lld:pubmed |
| pubmed-article:16091587 | pubmed:meshHeading | pubmed-meshheading:16091587... | lld:pubmed |
| pubmed-article:16091587 | pubmed:meshHeading | pubmed-meshheading:16091587... | lld:pubmed |
| pubmed-article:16091587 | pubmed:meshHeading | pubmed-meshheading:16091587... | lld:pubmed |
| pubmed-article:16091587 | pubmed:meshHeading | pubmed-meshheading:16091587... | lld:pubmed |
| pubmed-article:16091587 | pubmed:meshHeading | pubmed-meshheading:16091587... | lld:pubmed |
| pubmed-article:16091587 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16091587 | pubmed:articleTitle | Repetitive interactions observed in the crystal structure of a collagen-model peptide, [(Pro-Pro-Gly)9]3. | lld:pubmed |
| pubmed-article:16091587 | pubmed:affiliation | Faculty of Technology, Tokyo University of Agriculture & Technology, Koganei. | lld:pubmed |
| pubmed-article:16091587 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16091587 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
