SWISS-MODEL: homology modelling of protein structures and complexes
نویسندگان
چکیده
منابع مشابه
The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
MOTIVATION Homology models of proteins are of great interest for planning and analysing biological experiments when no experimental three-dimensional structures are available. Building homology models requires specialized programs and up-to-date sequence and structural databases. Integrating all required tools, programs and databases into a single web-based workspace facilitates access to homol...
متن کاملSWISS-MODEL: an automated protein homology-modeling server
SWISS-MODEL (http://swissmodel.expasy.org) is a server for automated comparative modeling of three-dimensional (3D) protein structures. It pioneered the field of automated modeling starting in 1993 and is the most widely-used free web-based automated modeling facility today. In 2002 the server computed 120 000 user requests for 3D protein models. SWISS-MODEL provides several levels of user inte...
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The theory of local homology modules was initiated by Matlis in 1974. It is a dual version of the theory of local cohomology modules. Mohammadi and Divaani-Aazar (2012) studied the connection between local homology and Gorenstein flat modules by using Gorenstein flat resolutions. In this paper, we introduce generalized local homology modules for complexes and we give several ways for computing ...
متن کاملHomology-based modeling of 3D structures of protein-protein complexes using alignments of modified sequence profiles.
Customary practice in predicting 3D structures of protein-protein complexes is employment of various docking methods when the structures of separate monomers are known a priori. The alternative approach, i.e. the template-based prediction with pure sequence information as a starting point, is still considered as being inferior mostly due to presumption that the pool of available structures of p...
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ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 2018
ISSN: 0305-1048,1362-4962
DOI: 10.1093/nar/gky427