On 07.01.2009, at 22:54, Jacob Keller wrote:
These cases, however, presuppose that one knows which type of case
one is dealing with. This could be done by guesswork and trial-and-
error, but does anybody know of an approach (e.g., a program) to
define the most reasonable way to think about a
I version of ESCET working in a pairwise fashion on different conformation
of the same structure or structures of similar proteins with different
sequences is also available as a web-server. The algorithm is called RAPIDO
and you can find it here:
webapps.embl-hamburg.de/rapido
And is described i
You can abuse/mis-use the TLSMD server from Ethan to analyse domain
movements and draw your conclusions accordingly, see here http://skuld.bmsc.washington.edu/~tlsmd/
Jürgen
On 7 Jan 2009, at 16:54, Jacob Keller wrote:
Dear Crystallographers,
I am sure that most here have dealt with the iss
This sounds like a job for a DDM (difference-distance matrix). This method
can detect very subtle conformational changes between a pair of protein
structures without performing a structural alignment. Once the areas of
change have been identified a traditional alignment can be performed using
the
On Wed, Jan 7, 2009 at 1:54 PM, Jacob Keller
wrote:
> I am sure that most here have dealt with the issue, when making
superpositions of conformationally-different structures,> of which regions
to align as references and which to call "mobile." Conformational changes
can range from very local (e.g.
Dear Crystallographers,
I am sure that most here have dealt with the issue, when making superpositions
of conformationally-different structures, of which regions to align as
references and which to call "mobile." Conformational changes can range from
very local (e.g., unwinding of a helix) to v
