CoDNaS 2.0: a comprehensive database of protein conformational diversity in the native state
| Autor: | María Silvina Fornasari, Gustavo Parisi, Alexander Miguel Monzon, Cristian Oscar Rohr |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Protein structure database Bioinformatics Protein Conformation media_common.quotation_subject Sequence (biology) Biology computer.software_genre General Biochemistry Genetics and Molecular Biology purl.org/becyt/ford/1 [https] Databases 03 medical and health sciences Protein structure Biological property Native state purl.org/becyt/ford/1.6 [https] Databases Protein Conformational isomerism media_common Flexibility (engineering) 030102 biochemistry & molecular biology Database Protein Proteins Search Engine 030104 developmental biology Database Update General Agricultural and Biological Sciences Conformational Diversity human activities computer Information Systems Diversity (politics) |
| Zdroj: | Database: The Journal of Biological Databases and Curation CONICET Digital (CONICET) Consejo Nacional de Investigaciones Científicas y Técnicas instacron:CONICET |
| ISSN: | 1758-0463 |
| DOI: | 10.1093/database/baw038 |
| Popis: | CoDNaS (conformational diversity of the native state) is a protein conformational diversitydatabase. Conformational diversity describes structural differences between conformersthat define the native state of proteins. It is a key concept to understand proteinfunction and biological processes related to protein functions. CoDNaS offers a well curateddatabase that is experimentally driven, thoroughly linked, and annotated. CoDNaS facilitatesthe extraction of key information on small structural differences based on proteinmovements. CoDNaS enables users to easily relate the degree of conformational diversitywith physical, chemical and biological properties derived from experiments on proteinstructure and biological characteristics. The new version of CoDNaS includes 70%of all available protein structures, and new tools have been added that run sequencesearches, display structural flexibility profiles and allow users to browse the database fordifferent structural classes. These tools facilitate the exploration of protein conformationaldiversity and its role in protein function. Fil: Monzón, Alexander. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina Fil: Rohr, Cristian Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Ecología, Genética y Evolución de Buenos Aires. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Ecología, Genética y Evolución de Buenos Aires; Argentina Fil: Fornasari, Maria Silvina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina Fil: Parisi, Gustavo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina |
| Databáze: | OpenAIRE |
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