Brahmachari, SK and Ananthanarayanan, VS (1979) Beta-turns in nascent procollagen are sites of posttranslational enzymatic hydroxylation of proline. In: PNAS, 76 (10). pp. 5119-5123.
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The selective hydroxylation of proline residues in nascent procollagen chains by prolyl hydroxylase (EC 188.8.131.52) can be understood in terms of the conformational feature of the -Pro-Gly-segments in linear peptides and globular proteins. The folded beta-turn conformation in such segments appears to be the conformational requirement for proline hydroxylation. The available data on the hydroxylation of native and synthetic substrates of prolyl hydroxylase are explained on the basis of the extent of beta-turn formation in them. Taken in conjunction with the conformational features of the hydroxyproline residue, our results bring out the conformational reason for the posttranslational proline hydroxylation which, it is proposed, leads to the "straightening" of the beta-turn segments into the linear triple-helical conformation.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to National Academy of Sciences.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||23 Sep 2010 09:21|
|Last Modified:||23 Sep 2010 09:21|
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