Stabilization of the collagen triple helix by O-methylation of hydroxyproline residues
- PMID: 18271593
- PMCID: PMC2802593
- DOI: 10.1021/ja800225k
Stabilization of the collagen triple helix by O-methylation of hydroxyproline residues
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References
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For a review, see:Raines RT. Protein Sci. 2006;15:1219–1225.
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Bella J, Eaton M, Brodsky B, Berman HM. Science. 1994;266:75–81.Bella J, Brodsky B, Berman HM. Structure. 1995;3:893–906.Miles CA, Burjanadze TV. Biophys. J. 2001;80:1480–1486.
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It is noteworthy that the frequency of Hyp could be too low to support such a water network in natural collagen. In the strands of human type-I collagen, an Xaa–Hyp–Gly sequence occurs in no more than four consecutive triads, and occurs in four consecutive triads only twice over >1000 residues.
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Holmgren SK, Taylor KM, Bretscher LE, Raines RT. Nature. 1998;392:666–667.Holmgren SK, Bretscher LE, Taylor KM, Raines RT. Chem. Biol. 1999;6:63–70.DeRider ML, Wilkens SJ, Waddell MJ, Bretscher LE, Weinhold F, Raines RT, Markley JL. J. Am. Chem. Soc. 2002;124:2497–2505.
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