Skip Navigation

This Article
Right arrow FREE Full Text (Print PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Labesse, G.
Right arrow Articles by Mornon, J.-P.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Labesse, G.
Right arrow Articles by Mornon, J.-P.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© Oxford University Press

P-SEA: a new efficient assignment of secondary structure from C{alpha} trace of proteins

G. Labesse 2, N. Colloc'h , J. Pothier 1 and J.-P. Mornon

Système Moléculaire et Biologie Structural, Laboratoire de Mineralogie-Cristallographie, Universités Paris 6/Paris 7, CNRS URA 09, case 115, 4, place Jussieu, 75252 Paris Cedex 05
1Atelier de BioInformatique, Institut Curie 11, rue Pierre et Marie Curie, 75231 Paris Cedex 05, France

2 To whom correspondence should be addressed

Motivation: The secondary structure is a key element of architectural organization in proteins. Accurate assignment of the secondary structure elements (SSE) (helix, strand, coil) is an essential step for the analysis and modelling of protein structure. Various methods have been proposed to assign secondary structure. Comparative studies of their results have shown some of their drawbacks, pointing out the difficulties in the task of SSE assignment.

Results: We have designed a new automatic method, named P-SEA, to assign efficiently secondary structure from the sole C{alpha} position. Some advantages of the new algorithm are discussed.

Availability: The program P-SEA is available by anonymous ftp: ftp.lmcp.jussieu.fr directory:pub/

Received on September 19, 1996; revised on December 30, 1996; accepted on January 3, 1997

Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Mol. Pharmacol.Home page
R. P. Riek, A. A. Finch, G. E. Begg, and R. M. Graham
Wide Turn Diversity in Protein Transmembrane Helices Implications for G-Protein-Coupled Receptor and Other Polytopic Membrane Protein Structure and Function
Mol. Pharmacol., April 1, 2008; 73(4): 1092 - 1104.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
M. Siaut, C. Zaros, E. Levivier, M.-L. Ferri, M. Court, M. Werner, I. Callebaut, P. Thuriaux, A. Sentenac, and C. Conesa
An Rpb4/Rpb7-Like Complex in Yeast RNA Polymerase III Contains the Orthologue of Mammalian CGRP-RCP
Mol. Cell. Biol., January 1, 2003; 23(1): 195 - 205.
[Abstract] [Full Text]

Home page
 Protein Sci.Home page
A. G. de Brevern, H. Valadie, S. Hazout, and C. Etchebest
Extension of a local backbone description using a structural alphabet: A new approach to the sequence-structure relationship
Protein Sci., December 1, 2002; 11(12): 2871 - 2886.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
A. R. Ortiz, C. E.M. Strauss, and O. Olmea
MAMMOTH (Matching molecular models obtained from theory): An automated method for model comparison
Protein Sci., November 1, 2002; 11(11): 2606 - 2621.
[Abstract] [Full Text] [PDF]

Home page
 Protein Eng Des SelHome page
M.N. Fodje and S. Al-Karadaghi
Occurrence, conformational features and amino acid propensities for the {pi}-helix
Protein Eng. Des. Sel., May 1, 2002; 15(5): 353 - 358.
[Abstract] [Full Text] [PDF]

Home page
 Protein Eng Des SelHome page
D. Znamenskiy, K. Le Tuan, A. Poupon, J. Chomilier, and J.-P. Mornon
{beta}-Sheet modeling by helical surfaces
Protein Eng. Des. Sel., June 1, 2000; 13(6): 407 - 412.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
G. Labesse, D. Ferrari, Z.-w. Chen, G.-L. Rossi, V. Kuusk, W. S. McIntire, and F. S. Mathews
Crystallographic and Spectroscopic Studies of Native, Aminoquinol, and Monovalent Cation-bound Forms of Methylamine Dehydrogenase from Methylobacterium extorquens AM1
J. Biol. Chem., October 2, 1998; 273(40): 25703 - 25712.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.