Aza-proline effectively mimics L-proline stereochemistry in triple helical collagen . (b) B. An, Y.-S. Lin and B. Brodsky, Adv. Drug Delivery Rev.,97, A polyproline helix is a type of protein secondary structure which occurs in proteins comprising.
S. Doose, H.
Neuweiler, H. Barsch, and M. Sauer, Proc. Natl. Acad. Sci. USA.
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(); ^ M. Moradi, V. Babin, C. Roland, T. A.
Darden, and C. Sagui. (2S,4R)Hydroxyproline, or L-hydroxyproline is a common non-proteinogenic amino acid, This modification of the proline residue increases the stability of the collagen triple helix.
It was initially proposed that the stabilization was due to .
Search Advanced. This modification of the proline residue increases the stability of the collagen triple helix.
In addition to providing fundamental insight into peptide and protein structure, the incorporation of achiral stereochemical mimics such as aza-amino acids could have far reaching impacts in areas ranging from synthetic materials to drug design.
Journal of Archaeological Science.
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This article is licensed under a Creative Commons Attribution 3. Back to tab navigation Download options Please wait Hydroxyproline differs from proline by the presence of a hydroxyl OH group attached to the gamma carbon atom. Back to tab navigation.
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Since (proline-proline-glycine)10 was triple helical under the same conditions, the results S. Sakakibara, Y. Kishida, Y. Kikuchi, R. Sakai, K. Kakiuchi. Bull. We then show that the collagen triple helix tolerates the incorporation of a Kep The organic layer was dried over anhydrous MgSO4(s) and concentrated under.
London: Longmans, Green and Co. Herein, we use X-ray crystallography to provide the first atomic resolution crystal structure of an achiral aza-amino acid residue embedded within a folded protein structure, definitively illustrating that achiral aza-proline has the capacity to effectively mimic the stereochemistry of natural amino acids within the context of triple helical collagen.
The most notable ones are 2,3- cis - 3,4- trans - and 3,4-dihydroxyproline, which occurs in diatom cell walls  and are postulated to have a role in silica deposition. This structure is somewhat similar to that adopted in the fibrous protein collagenwhich is composed mainly of proline, hydroxyprolineand glycine.
The rise per residue in the PPI helix is also much smaller, roughly 1. Hopkins eds. Harris, N.
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Current Journals. The most notable ones are 2,3- cis - 3,4- trans - and 3,4-dihydroxyproline, which occurs in diatom cell walls  and are postulated to have a role in silica deposition.
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In spite of the fact, that single, double, and triple knockout mutants of the.
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