• Publications
  • Influence
Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution.
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 consensusExpand
  • 787
  • 17
Molecular structure of the collagen triple helix.
The molecular conformation of the collagen triple helix confers strict amino acid sequence constraints, requiring a (Gly-X-Y)(n) repeating pattern and a high content of imino acids. The increasingExpand
  • 411
  • 12
Hydration structure of a collagen peptide.
BACKGROUND The collagen triple helix is a unique protein motif defined by the supercoiling of three polypeptide chains in a polyproline II conformation. It is a major domain of all collagen proteinsExpand
  • 490
  • 11
  • PDF
Sequence dependent conformational variations of collagen triple-helical structure
The 2 Å crystal structure reported here of the collagen-like model peptide, T3-785, provides the first visualization of how the sequence of collagen defines distinctive local conformationalExpand
  • 261
  • 9
Prediction of Collagen Stability from Amino Acid Sequence*
An algorithm was derived to relate the amino acid sequence of a collagen triple helix to its thermal stability. This calculation is based on the triple helical stabilization propensities ofExpand
  • 255
  • 9
  • PDF
The collagen triple-helix structure.
  • B. Brodsky, J. Ramshaw
  • Chemistry, Medicine
  • Matrix biology : journal of the International…
  • 1 March 1997
Recent advances, principally through the study of peptide models, have led to an enhanced understanding of the structure and function of the collagen triple helix. In particular, the first crystalExpand
  • 383
  • 8
Gly-X-Y tripeptide frequencies in collagen: a context for host-guest triple-helical peptides.
The collagen triple-helix consists of a repeating (Gly-X-Y)n sequence. In theory, there are more than 400 possible Gly-X-Y triplets, but analysis of sequences from fibrillar and nonfibrillarExpand
  • 235
  • 8
Amino acid propensities for the collagen triple-helix.
Determination of the tendencies of amino acids to form alpha-helical and beta-sheet structures has been important in clarifying stabilizing interactions, protein design, and the protein foldingExpand
  • 262
  • 6
Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair.
The crystal structure of the triple-helical peptide, (Pro-Hyp-Gly)(4)-Glu-Lys-Gly-(Pro-Hyp-Gly)(5) has been determined to 1.75 A resolution. This peptide was designed to examine the effect of a pairExpand
  • 162
  • 5
Mechanism of Stabilization of a Bacterial Collagen Triple Helix in the Absence of Hydroxyproline*
The Streptococcus pyogenes cell-surface protein Scl2 contains a globular N-terminal domain and a collagen-like domain, (Gly-Xaa-X′aa)79, which forms a triple helix with a thermal stability close toExpand
  • 102
  • 5
  • PDF