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Treffer: Helix interaction tool (HIT) : a web-based tool for analysis of helix-helix interactions in proteins

Title:
Helix interaction tool (HIT) : a web-based tool for analysis of helix-helix interactions in proteins
Source:
Bioinformatics (Oxford. Print). 22(22):2735-2738
Publisher Information:
Oxford: Oxford University Press, 2006.
Publication Year:
2006
Physical Description:
print, 18 ref
Original Material:
INIST-CNRS
LGMI
Document Type:
Fachzeitschrift Article
File Description:
text
Language:
English
Author Affiliations:
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, United States
ISSN:
1367-4803
Rights:
Copyright 2007 INIST-CNRS
CC BY 4.0
Sauf mention contraire ci-dessus, le contenu de cette notice bibliographique peut être utilisé dans le cadre d’une licence CC BY 4.0 Inist-CNRS / Unless otherwise stated above, the content of this bibliographic record may be used under a CC BY 4.0 licence by Inist-CNRS / A menos que se haya señalado antes, el contenido de este registro bibliográfico puede ser utilizado al amparo de una licencia CC BY 4.0 Inist-CNRS
Notes:
Biological sciences. Generalities. Modelling. Methods

Generalities in biological sciences
Accession Number:
edscal.18300196
Database:
PASCAL Archive

Weitere Informationen

Motivation: In many proteins, helix-helix interactions can be critical to establishing protein conformation (folding) and dynamics, as well as determining associations between protein units. However, the determination of a set of rules that guide helix-helix interaction has been elusive. In orderto gain furtherinsight into the helix-helix interface, we have developed a comprehensive package of tools for analyzing helix-helix packing in proteins. These tools are available at http://helix. gersteinlab.org. They include quantitative measures of the helix interaction surface area and helix crossing angle, as well as several methods for visualizing the helical interaction. These methods can be used for analysis of individual protein conformations or to gain insight into dynamic changes in helix interactions. For the latter purpose, a direct interface from entries in the Molecular Motions Database to the HIT site has been provided.