[Blends-commit] r3370 - /projects/med/trunk/debian-med/tasks/bio

[tille at users.alioth.debian.org]

Author: tille
Date: Mon May 28 15:35:26 2012
New Revision: 3370

URL: http://svn.debian.org/wsvn/blends/?sc=1&rev=3370
Log:
Remove now redundant information

Modified:
    projects/med/trunk/debian-med/tasks/bio

Modified: projects/med/trunk/debian-med/tasks/bio
URL: http://svn.debian.org/wsvn/blends/projects/med/trunk/debian-med/tasks/bio?rev=3370&op=diff
==============================================================================
--- projects/med/trunk/debian-med/tasks/bio (original)
+++ projects/med/trunk/debian-med/tasks/bio Mon May 28 15:35:26 2012
@@ -393,6 +393,10 @@
  free.  Thus a change might be possible
 
 Depends: proalign
+
+Depends: sap
+Remark: Precondition for T-Coffee
+ see http://wiki.debian.org/DebianMed/TCoffee
 
 X-Mark: The information below needs to be checked whether it can be obtained from Vcs or needs to stay here
 
@@ -2508,33 +2512,6 @@
  technique for constructing a multiple alignment from pairwise
  comparisons, developed by Ariel Schwartz in  "Posterior Decoding Methods
  for Optimization and Control of Multiple Alignments."
-Remark: Precondition for T-Coffee
- see http://wiki.debian.org/DebianMed/TCoffee
-
-Depends: sap
-Homepage: http://mathbio.nimr.mrc.ac.uk/wiki/Software#SAP
-License: GPL v3
-Enhances: t-coffee
-Pkg-Description: Pairwise protein structure alignment via double dynamic programming
- In contrast to DNA, proteins exhibit an apparently unlimited variety of
- structure. This is a necessary requirement of the vast array of
- differing functions that they perform in the maintainance of life,
- again, in contrast to the relatively static archival function of DNA.
- Not only do we observe a bewildering variety of form but even within a
- common structure, there is variation in the lengths and orientation
- substructures. Such variation is both a reflection on the very long time
- periods over which some structures have diverged and also a consequence
- of the fact that proteins cannot be completely rigid bodies but must
- have flexibility to accommodate the structural changes that are almost
- always necessary for them to perform their functions. These aspects make
- comparing structure and finding structural similarity over long
- divergence times very difficult. Indeed, computationally, the problem of
- recognizing similarity is one of three-dimensional pattern recognition,
- which is a notoriously difficult problem for computers to perform. In
- this chapter, guidance is provided on the use of a flexible structure
- comparison method that overcomes many of the problems of comparing
- protein structures that may exhibit only weak similarity.
-Published-URL: http://www.springerprotocols.com/Abstract/doi/10.1385/1-59259-368-2:19
 Remark: Precondition for T-Coffee
  see http://wiki.debian.org/DebianMed/TCoffee