Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution.
Abstract
The structure of a protein triple helix has been determined at 1.9 angstrom resolution by x-ray crystallographic studies of a collagen-like peptide containing a single substitution of the consensus sequence. This peptide adopts a triple-helical structure that confirms the basic features determined from fiber diffraction studies on collagen: supercoiling of polyproline II helices and interchain hydrogen bonding that follows the model II of Rich...
Paper Details
Title
Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution.
Published Date
Oct 7, 1994
Journal
Volume
266
Issue
5182
Pages
75 - 81
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