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Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution.
The structure of a protein triple helix has been determined by x-ray crystallographic studies of a collagen-like peptide containing a single substitution of the consensus sequence, which adopts a triple-helical structure that confirms the basic features determined from fiber diffraction studies on collagen.
Molecular structure of the collagen triple helix.
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 conformational
Gly-X-Y tripeptide frequencies in collagen: a context for host-guest triple-helical peptides.
A set of host-guest peptides was designed to contain the most common nonpolar and charged triplets found in collagen and provides a starting point for establishing a stability scale to predict the relative stability of important collagen regions, such as the matrix metalloproteinase cleavage site or binding sites.
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 of
Supercoiled Protein Motifs: The Collagen Triple-Helix and the α-Helical Coiled Coil
The collagen triple-helix and the alpha-helical coiled coil represent the two basic supercoiled multistranded protein motifs. Originally they were characterized in fibrous proteins, but have been
Amino acid propensities for the collagen triple-helix.
A complete scale of amino acid propensities for the collagen triple-helix conformation with its Gly-X-Y repeating sequence is determined for the first time, providing a first step in defining sequence-dependent variations in local triple- Helix stability and binding.
The collagen triple-helix structure.
  • B. Brodsky, J. Ramshaw
  • Biology, Chemistry
    Matrix biology : journal of the International…
  • 1 March 1997
Defining Requirements for Collagenase Cleavage in Collagen Type III Using a Bacterial Collagen System*
The recombinant bacterial-human collagen system characterized here is a good model to investigate the specificity and mechanism of action of collagenases.