Linked Life Data

16903677

Source:http://linkedlifedata.com/resource/pubmed/id/16903677

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2006-8-14
pubmed:abstractText
The manufacture of parchment from animal skin involves processes that remove hair, fats, and other macromolecules. Although it is well understood that the collagen fibers "open up" during processing, this study uses small and wide-angle X-ray diffraction to measure quantitatively the changes induced at the nanoscopic and microscopic levels. The axial rise per residue distance within the collagen molecules is unaffected by salt and lime treatments. Salting of the hides appears to remove noncollagenous materials. The intermolecular lateral packing distance between the hydrated collagen molecules (1.4 nm) increases after salting ( approximately 1.5 nm) and liming ( approximately 1.55 nm); drying is responsible for a reduction to approximately 1.2 nm in all samples. The axial staggered array (d spacing) is reduced by 1 nm after liming and is unaffected by drying. The average fibril diameter increases from 103.2 to 114.5 nm following liming, and the fibril-to-fibril distance increases from 122.6 to 136.1 nm.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1525-7797
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2321-6
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
X-ray diffraction study into the effects of liming on the structure of collagen.
pubmed:affiliation
Biophysics Division, School of Optometry and Vision Sciences, University of Cardiff, Redwood Building, King Edward VII Avenue, Cathays Park, Cardiff, Wales, United Kingdom. MaxwellCA@cardiff.ac.uk
pubmed:publicationType
Journal Article