منابع مشابه
Understanding and Engineering the Collagen Triple Helix
UNDERSTANDING AND ENGINEERING THE COLLAGEN TRIPLE HELIX Matthew Donald Shoulders Under the supervision of Professor Ronald T. Raines At the University of Wisconsin-Madison This thesis presents a hypothesis-driven approach to collagen research that integrates the power of organic chemistry with the tools of biophysics to enhance our understanding of proline conformation and collagen structure an...
متن کاملThioamides in the collagen triple helix.
To probe noncovalent interactions within the collagen triple helix, backbone amides were replaced with a thioamide isostere. This subtle substitution is the first in the collagen backbone that does not compromise thermostability. A triple helix with a thioamide as a hydrogen bond donor was found to be more stable than triple helices assembled from isomeric thiopeptides.
متن کاملMacrocyclic scaffold for the collagen triple helix.
[structure: see text] Three strands of natural collagen are linked by covalent bonds prior to their folding into a triple helix. We report on a synthetic collagen in which the strands are pendent on a rigid macrocyclic scaffold of C(3) symmetry. The scaffold confers substantial conformational stability upon the collagen triple helix and makes its folding independent of concentration, both desir...
متن کاملCTHRC1 (Collagen Triple Helix Repeat Containing 1)
Collagen Triple Helix Repeat Containing-1, CTHRC1, is a 30kDa secreted protein that has the ability to inhibit collagen matrix synthesis. CTHRC1 is glycosylated and retains a signal sequence consistent with it being secreted from the cell. Activity of the protein is reliant on removal of the propeptide and while CTHRC1 does not contain a predictable consensus propeptide cleavage site, there is ...
متن کاملCollagen structure: the Madras triple helix and the current scenario.
This year marks the 50th anniversary of the coiled-coil triple helical structure of collagen, first proposed by Ramachandran's group from Madras. The structure is unique among the protein secondary structures in that it requires a very specific tripeptide sequence repeat, with glycine being mandatory at every third position and readily accommodates the imino acids proline/hydroxyproline, at the...
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ژورنال
عنوان ژورنال: Nature
سال: 1974
ISSN: 0028-0836,1476-4687
DOI: 10.1038/249406a0