Pierre THEVENET wrote:
In most cases (it is form predicted structures) if the bonds is not
formes, the S atoms are at the opposite side of the backbone. And I work
on peptides, so the length of the structure isn't that big (50 residues max)
Well, if you try the distance restraint approach, I'd do it in the absence of
any solvent since there likely will be rather large structural changes (and thus
very fast protein-solvent clashes as the restraints are satisfied), unless the
peptide is pretty compact. Really short MD should tell you if this will even be
feasible.
-Justin
--
========================================
Justin A. Lemkul
Ph.D. Candidate
ICTAS Doctoral Scholar
MILES-IGERT Trainee
Department of Biochemistry
Virginia Tech
Blacksburg, VA
jalemkul[at]vt.edu | (540) 231-9080
http://www.bevanlab.biochem.vt.edu/Pages/Personal/justin
========================================
--
gmx-users mailing list [email protected]
http://lists.gromacs.org/mailman/listinfo/gmx-users
Please search the archive at
http://www.gromacs.org/Support/Mailing_Lists/Search before posting!
Please don't post (un)subscribe requests to the list. Use the
www interface or send it to [email protected].
Can't post? Read http://www.gromacs.org/Support/Mailing_Lists
