Collagen probably isn't a great example as hydroxylation of proline in collagen enhances the thermal stability of collagen, it doesn't really "induce" collagen structure, as unhydroxylated (pro-pro-gly)n also form the canonical triple-helical structure. Unless, of course, your looking at temperatures where hydroxylated peptides form helices where unmodified ones don't.
 
Paul..
 
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Dr. Paul A. McEwan
Office B55
Centre for Biomolecular Science
University of Nottingham
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From: CCP4 bulletin board on behalf of Tom Murray-Rust
Sent: Thu 04/03/2010 11:22 AM
To: [log in to unmask]
Subject: Re: [ccp4bb] Post-translational modification induced strcture

Hi Miles -

I would say a good example of that phenomenon is collagen, where
hydroxylation of the prolyl residues alows the polypeptide to adopt
its helical conformation. In that case it is the fact there is an
electronegative substituent on the prolyl ring that biases it into a
particular conformation, which is perfect for forming helices (and
doesn't involve a cofactor).

Best Regards,

Tom

--
Dr. Tom Murray-Rust
Department of Haematology
Cambridge Institute of Medical Research
Wellcome Trust/MRC Building, Hills Road
Cambridge CB2 0XY



On Thu, Mar 4, 2010 at 10:45 AM, Miles Pufall <[log in to unmask]> wrote:
> Dear All -
> Does anyone have some good examples where a post-translational modification
> has induced local structure?  I'm particularly thinking of structure induced
> by the modification only and not something multi-step like a modification
> that recruits a cofactor that induces structure.
> Thanks!
> Miles
> Miles Pufall
> Postdoctoral Fellow, UC San Francisco
> 600 16th Street, Genentech Hall S-574
> San Francisco, California 94158-2517
>
>


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