Crystal and Molecular Structure of a Collagen-Like Peptide at 1.9 Å Resolution

scientific article published on October 7, 1994

Crystal and Molecular Structure of a Collagen-Like Peptide at 1.9 Å Resolution is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1126/SCIENCE.7695699
P953full work available at URLhttps://www.science.org/doi/pdf/10.1126/science.7695699
P3181OpenCitations bibliographic resource ID629127
P698PubMed publication ID7695699

P50authorHelen M. BermanQ7441
P2093author name stringB. Brodsky
M. Eaton
J. Bella
P2860cites workProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coilQ27655682
Crystallographic R factor refinement by molecular dynamicsQ27860942
A graphics model building and refinement system for macromoleculesQ29642804
The structure of collagenQ33969096
Chain conformation in the collagen moleculeQ34213877
Crystal and molecular structure of a collagen-like polypeptide (Pro-Pro-Gly)10Q34284709
Molecular conformation and packing in collagen fibrilsQ38580064
Circular-dichroism and electron-microscopy studies of human subcomponent C1q before and after limited proteolysis by pepsinQ40030966
Type I macrophage scavenger receptor contains alpha-helical and collagen-like coiled coilsQ41744280
Synthesis of (Pro-Hyp-Gly) n of defined molecular weights. Evidence for the stabilization of collagen triple helix by hydroxypyrolineQ48000402
Structural model of the collagen-like region of C1q comprising the kink region and the fibre-like packing of the six triple helices.Q52495611
Accurate bond and angle parameters for X-ray protein structure refinementQ56485700
Structure of CollagenQ59057538
The triple helix in equilibrium with coil conversion of collagen-like polytripeptides in aqueous and nonaqueous solvents. Comparison of the thermodynamic parameters and the binding of water to (L-Pro-L-Pro-Gly)n and (L-Pro-L-Hyp-Gly)nQ67555188
Nuclear magnetic resonance and circular dichroism studies of a triple-helical peptide with a glycine substitutionQ68122137
Single crystals of (Pro-Pro-Gly) 10, a synthetic polypeptide model of collagenQ70410012
Electrostatic interactions in collagen-like triple-helical peptidesQ72015659
Characterization of collagen-like peptides containing interruptions in the repeating Gly-X-Y sequenceQ72551704
Two-dimensional NMR assignments and conformation of (Pro-Hyp-Gly)10 and a designed collagen triple-helical peptideQ72850799
The molecular structure of collagenQ79062176
Systematic analysis of structural data as a research technique in organic chemistryQ116981303
P433issue5182
P407language of work or nameEnglishQ1860
P921main subjectmolecular geometryQ911331
P304page(s)75-81
P577publication date1994-10-07
P1433published inScienceQ192864
P1476titleCrystal and molecular structure of a collagen-like peptide at 1.9 A resolution
Crystal and Molecular Structure of a Collagen-Like Peptide at 1.9 Å Resolution
P478volume266

Reverse relations

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Q28285338The peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is a tetratricopeptide repeat domain with functional aromatic residues
Q91829343The predominant roles of the sequence periodicity in the self-assembly of collagen-mimetic mini-fibrils
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