[med-svn] r11786 - trunk/packages/norsp/trunk/debian

[Eva Reisinger]

Author: reisinger-guest
Date: 2012-07-13 12:32:44 +0000 (Fri, 13 Jul 2012)
New Revision: 11786

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 12:29:08 UTC (rev 11785)
+++ trunk/packages/norsp/trunk/debian/control	2012-07-13 12:32:44 UTC (rev 11786)
@@ -12,5 +12,18 @@
 Depends: ${misc:Depends}
 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. 
-
+ 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.