[med-svn] r11787 - trunk/packages/norsp/trunk/debian

Eva Reisinger reisinger-guest at alioth.debian.org
Fri Jul 13 12:33:26 UTC 2012


Author: reisinger-guest
Date: 2012-07-13 12:33:26 +0000 (Fri, 13 Jul 2012)
New Revision: 11787

Modified:
   trunk/packages/norsp/trunk/debian/control
Log:
change controll file

Modified: trunk/packages/norsp/trunk/debian/control
===================================================================
--- trunk/packages/norsp/trunk/debian/control	2012-07-13 12:32:44 UTC (rev 11786)
+++ trunk/packages/norsp/trunk/debian/control	2012-07-13 12:33:26 UTC (rev 11787)
@@ -13,17 +13,17 @@
 Recommends: pp-popularity-contest, profphd, profphd-utils, ncoils (>= 2002-3)
 Description: predictor of NOn-Regular Secondary Structure 
  Many structurally flexible regions play important roles in biological
-processes. It has been shown that extended loopy regions are very abundant in
-nature, and that they are evolutionarily conserved. NORSp is a publicly
-available predictor for disordered regions in protein. Specifically, it
-predicts long regions with no regular secondary structure. Upon user
-submission of protein sequence, NORSp will analyse the protein about its
-secondary structure, and presence of transmembrane helices and coiled-coil. It
-will then return e-mail to user about the presence and position of disordered
-regions.NORSp can be useful for biologists in several ways. For example,
-crystallographers can check whether their proteins contain NORS regions and
-make the decision about whether to proceed with the experiments since NORS
-proteins may be difficult to crystallise, as demonstrated by the their low
-occurrence in PDB. Biologists interested in protein structure-function
-relationship may also find it interesting to verify whether the
-protein-protein interaction sites coincide with NORS region.
+ processes. It has been shown that extended loopy regions are very abundant in
+ nature, and that they are evolutionarily conserved. NORSp is a publicly
+ available predictor for disordered regions in protein. Specifically, it
+ predicts long regions with no regular secondary structure. Upon user
+ submission of protein sequence, NORSp will analyse the protein about its
+ secondary structure, and presence of transmembrane helices and coiled-coil. It
+ will then return e-mail to user about the presence and position of disordered
+ regions.NORSp can be useful for biologists in several ways. For example,
+ crystallographers can check whether their proteins contain NORS regions and
+ make the decision about whether to proceed with the experiments since NORS
+ proteins may be difficult to crystallise, as demonstrated by the their low
+ occurrence in PDB. Biologists interested in protein structure-function
+ relationship may also find it interesting to verify whether the
+ protein-protein interaction sites coincide with NORS region.




More information about the debian-med-commit mailing list