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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Chapman, J. A. | en |
| dc.contributor.author | Tzaphlidou, M. | en |
| dc.contributor.author | Meek, K. M. | en |
| dc.contributor.author | Kadler, K. E. | en |
| dc.date.accessioned | 2015-11-24T19:42:16Z | - |
| dc.date.available | 2015-11-24T19:42:16Z | - |
| dc.identifier.issn | 0892-0354 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/24615 | - |
| dc.rights | Default Licence | - |
| dc.subject | Amino Acid Sequence | en |
| dc.subject | Animals | en |
| dc.subject | Collagen/*analysis/ultrastructure | en |
| dc.subject | Microscopy, Electron | en |
| dc.subject | Models, Biological | en |
| dc.subject | Molecular Sequence Data | en |
| dc.subject | Preservation, Biological | en |
| dc.subject | *Staining and Labeling | en |
| dc.title | The collagen fibril--a model system for studying the staining and fixation of a protein | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/1715773 | - |
| heal.identifier.secondary | http://ac.els-cdn.com/089203549090018N/1-s2.0-089203549090018N-main.pdf?_tid=0dd8c10bbb14bad627895b7b6b70094c&acdnat=1333105253_73acf5a350e70f0654322afa728121f9 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.publicationDate | 1990 | - |
| heal.abstract | A collagen fibril is made up of long rod-like molecules regularly D-staggered with respect to one another. This means that (i) its axially projected fine structure, resolvable to approximately 2 nm in electron micrographs, repeats D-periodically (D = 67 nm), and (ii) the amino acid residues contributing to each element of the fine structure can be inferred from sequence data. Electron-optical data from a fibril D-period can can therefore be correlated directly with chemical data. Such correlations confirm the electrostatic nature of the staining reaction when a fibril is positively stained. After negative staining, the principal factor determining the small-scale distribution of stain is local exclusion by 'bulky' amino acid side-chains. ('Bulkiness' is the average cross-sectional area, or 'plumpness', of a side-chain.) A small superimposed positive staining contribution can also be detected. Fixation of collagen by aldehydes and diimidoesters occurs via an initial reaction with lysyl (and hydroxylsyl) side-chains and alpha-amino groups, followed by secondary cross-linking reactions that differ from fixative to fixative. These secondary reactions determine the nature and abundance of the cross-links and the extent to which they influence subsequent staining behaviour. | en |
| heal.journalName | Electron Microsc Rev | en |
| heal.journalType | peer-reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Chapman-1990-The collagen fibril-.pdf | 5.34 MB | Adobe PDF | View/Open Request a copy |
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