The influence of water, lanolin, urea, proline, paraffin and fatliquor on collagen D-spacing in leather
Author:
Affiliation:
1. Australian Synchrotron
2. Melbourne
3. Australia
4. School of Engineering and Advanced Technology
5. Massey University
6. Palmerston North
7. New Zealand
8. Leather and Shoe Research Association
Abstract
Water, lanolin and Lipsol interact with collagen to alter the structure at the fibrillar scale.
Funder
Australian Synchrotron
Ministry of Business, Innovation and Employment
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemical Engineering,General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2017/RA/C7RA05560A
Reference25 articles.
1. Gly-X-Y Tripeptide Frequencies in Collagen: A Context for Host–Guest Triple-Helical Peptides
2. Collagen Structure and Stability
3. Crystal and Molecular Structure of a Collagen-Like Peptide at 1.9 Å Resolution
4. Cross-linkage sites in type I collagen fibrils studied by neutron diffraction
5. Fibrillar Structure and Mechanical Properties of Collagen
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