D
David S. Moss
Researcher at Birkbeck, University of London
Publications - 117
Citations - 28493
David S. Moss is an academic researcher from Birkbeck, University of London. The author has contributed to research in topics: Clostridium perfringens & Major histocompatibility complex. The author has an hindex of 38, co-authored 117 publications receiving 27038 citations. Previous affiliations of David S. Moss include Laboratory of Molecular Biology & University of London.
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PROCHECK: a program to check the stereochemical quality of protein structures
TL;DR: The PROCHECK suite of programs as mentioned in this paper provides a detailed check on the stereochemistry of a protein structure and provides an assessment of the overall quality of the structure as compared with well refined structures of the same resolution.
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Main-chain bond lengths and bond angles in protein structures.
TL;DR: The main-chain bond lengths and bond angles of protein structures are analysed as a function of resolution and differences in means are found to be highly statistically significant, suggesting that the different target values used by the different methods leave their imprint on the structures they refine.
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The molecular structure and stability of the eye lens: x-ray analysis of gamma-crystallin II.
Tom L. Blundell,Peter F. Lindley,Linda Miller,David S. Moss,Christine Slingsby,Ian J. Tickle,Bill Turnell,Graeme Wistow +7 more
TL;DR: The three-dimensional structure of the eye lens protein, bovine gamma-crystallin II, has been determined at 2.6 A resolution as discussed by the authors, and the protein has a tow domain beta-structure, folded into four remarkably similar 'Greed key' motifs, and shows the highest internal symmetry.
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X-ray analysis of the eye lens protein γ-II crystallin at 1·9 Å resolution
Graeme Wistow,Bill Turnell,Lesley Summers,Christine Slingsby,David S. Moss,Linda Miller,Peter F. Lindley,Tom L. Blundell +7 more
TL;DR: In this paper, the X-ray structure analysis and refinement at 1·9 A resolution of calf γ-II crystallin, a lens-specific protein, has been reported, which has a symmetrical, hierarchical structure of two globular domains each comprising two similar “Greek key” motifs, consecutive along the polypeptide chain, and related by a pseudo 2-fold axis.
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Conformational flexibility in a small globular hormone: x-ray analysis of avian pancreatic polypeptide at 0.98-A resolution.
I.D. Glover,Illyas Haneef,J. E. Pitts,Steve P. Wood,David S. Moss,Ian J. Tickle,Tom L. Blundell +6 more
TL;DR: For the first time, six‐parameter anisotropic thermal ellipsoids have been refined for each atom; these define the directions of the molecular motions in the polypeptide, indicating concerted vibrations.