gerard at rigel.bmc.uu.se (Gerard Kleijwegt) writes:
>And how many experimental observations went into that molecular
>dynamics simulation ???
Quite a lot - ... the X-ray structure was used as input to
the program ;-)
And what was that about needing 80% identity to get a reasonable
comparative model - is it my imagination, or is your estimate of the
required sequence simliarity going up!
For those that don't know, and aren't able to persuade a crystallographer
or NMR spectroscopist to solve the structure of their protein - there are
NO examples of proteins more than 100 residue in length and that share 30%
identity or more, that don't have essentially the same folds. If you've
got more than 50% identity, you probably won't even see too many shifts in
structure of the core. You can easily build "OK" models in these cases.
-- Simon
_________________________________________________________________________
|| ,_ o Simon M. Brocklehurst,
| / //\, Oxford Centre for Molecular Sciences
| \>> | Department of Biochemistry, University of Oxford,
| \\, Oxford, UK.
| E-mail: smb at bioch.ox.ac.uk| WWW: http://nmra.ocms.ox.ac.uk/~smb/|________________________________________________________________________
