[Date Prev][Date Next][Thread Prev][Thread Next][Date Index][Thread Index]
Ideal helices
- To: modeller_usage <modeller_usage@listsrv.ucsf.edu>
- Subject: Ideal helices
- From: Dan Thomas Major <majord AT mail.biu.ac.il>
- Date: Tue, 18 Jun 2002 13:43:17 +0300
- Organization: Bar-Ilan University
Hi,
I'm modelling G-protein coupled receptors using rhodopsin as a template.
When I compare the Ramachandran plot of the models vs that of rhodopsin,
the models have much more ideal helices than the rhodopsin X-ray structure
(2.8 A).
Is this because:
1) The homology is relatively low (20-30%) and the distance constraints
receive a low weight in the pdf function??
2) The helices in rhodopsin are less regular than the globular proteins
used in the pdf parametrization??
3) None of the above...
Sincerely,
Dan
--
Dan Thomas Major (at Dr. B. Fischer's lab)
Bar-Ilan University
Ramat-Gan, Israel
Phone: 972-3-5317785
Fax: 972-3-5348730