Two States of the Triple Helix in the Thermal Transition of the Collagen Model Peptide (Pro-Pro-Gly)10
Author:
Publisher
Informa UK Limited
Subject
Molecular Biology,General Medicine,Structural Biology
Link
http://www.tandfonline.com/doi/pdf/10.1080/10256018808623883
Reference28 articles.
1. Information contained in the amino acid sequence of theα1(I)-chain of collagen and its consequences upon the formation of the triple helix, of fibrils and crosslinks
2. Crystal and Molecular Structure of a Collagen-Like Peptide at 1.9 Å Resolution
3. X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly)
4. Structure Analysis of a Collagen-Model Peptide with a (Pro-Hyp-Gly) Sequence Repeat
5. Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3
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1. Thermal Denaturation of Type I Collagen Fibrils Investigated with Vibrational Circular Dichroism Spectroscopy;KOBUNSHI RONBUNSHU;2015
2. Comparative NMR Analysis of Collagen Triple Helix Organization from N- to C-Termini;Biomacromolecules;2014-12-10
3. Site-Directed Spin Labeling of a Collagen Mimetic Peptide;Chemistry - A European Journal;2013-11-22
4. The effect of purity upon the triple-helical stability of collagenous peptides;Biomaterials;2011-09
5. Thermal effects of added propanol on the helix–coil transition of (Pro-Pro-Gly)10 in D2O solution: An NMR study;Chemical Physics Letters;2010-05
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