Dear Jorge,

It sounds like you want to estimate the 'pitch' parameter of a coiled coil.
You can extract that information from the structure using TWISTER program,
a server is available here:
https://pharm.kuleuven.be/apps/biocryst/twister.php
The alpha-helical chains need to be in-register, i.e. the "parallel"
residues need to have the same residue numbers  (if that's not the case
you'll need to renumber the chains before submitting).

Kind regards,
Dmytro.

On Tue, Aug 28, 2018 at 6:03 AM, Jorge Iulek <[email protected]> wrote:

> Dear all,
>
>
>     I am working currently on a structure that, nicely, presents two
> different orientations between its domains when one compares monomers of
> the tetramer in the asymmetric unit.
>
>     I notice, in this nature gift, that a helix, probably central (in its
> role) for the relation (orientation) between the two domains,  assumes
> different relation to other one (helix, that belongs to one of the domains)
> such that they are (significantly) more or less "coiled-coiled"one to
> another, once the domains are in the "close" or "open" conformation. We
> have already analyzed the hydrogen bonds and salt bridges that are
> disrupted (or formed) due to the different (domain and helix) conformations.
>
>     I wonder whether there is a metric (easy to evaluate) to characterize
> how much the two helix are "around each other" (id est, how much
> "coiled-coiled" they are) and, preferably, a software to calculate this
> metric.
>
>     Thank you,
>
>
> Jorge
>
> State University of Ponta Grossa
>
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