CoDNaS 2.0: A comprehensive database of protein conformational diversity in the native state

CoDNaS (conformational diversity of the native state) is a protein conformational diversity database. Conformational diversity describes structural differences between conformers that define the native state of proteins. It is a key concept to understand protein function and biological processes rel...

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Detalles Bibliográficos
Autores principales: Monzon, A.M., Rohr, C.O., Fornasari, M.S., Parisi, G.
Formato: JOUR
Materias:
protein
chemistry
protein conformation
protein database
search engine
Databases, Protein
Protein Conformation
Proteins
Search Engine
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_17580463_v2016_n_p_Monzon
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_17580463_v2016_n_p_Monzon
record_format dspace
spelling todo:paper_17580463_v2016_n_p_Monzon2023-10-03T16:32:43Z CoDNaS 2.0: A comprehensive database of protein conformational diversity in the native state Monzon, A.M. Rohr, C.O. Fornasari, M.S. Parisi, G. protein chemistry protein conformation protein database search engine Databases, Protein Protein Conformation Proteins Search Engine CoDNaS (conformational diversity of the native state) is a protein conformational diversity database. Conformational diversity describes structural differences between conformers that define the native state of proteins. It is a key concept to understand protein function and biological processes related to protein functions. CoDNaS offers a well curated database that is experimentally driven, thoroughly linked, and annotated. CoDNaS facilitates the extraction of key information on small structural differences based on protein movements. CoDNaS enables users to easily relate the degree of conformational diversity with physical, chemical and biological properties derived from experiments on protein structure and biological characteristics. The new version of CoDNaS includes 70% of all available protein structures, and new tools have been added that run sequence searches, display structural flexibility profiles and allow users to browse the database for different structural classes. These tools facilitate the exploration of protein conformational diversity and its role in protein function. © The Author(s) 2016. Published by Oxford University Press. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_17580463_v2016_n_p_Monzon
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic protein
chemistry
protein conformation
protein database
search engine
Databases, Protein
Protein Conformation
Proteins
Search Engine
spellingShingle protein
chemistry
protein conformation
protein database
search engine
Databases, Protein
Protein Conformation
Proteins
Search Engine
Monzon, A.M.
Rohr, C.O.
Fornasari, M.S.
Parisi, G.
CoDNaS 2.0: A comprehensive database of protein conformational diversity in the native state
topic_facet protein
chemistry
protein conformation
protein database
search engine
Databases, Protein
Protein Conformation
Proteins
Search Engine
description CoDNaS (conformational diversity of the native state) is a protein conformational diversity database. Conformational diversity describes structural differences between conformers that define the native state of proteins. It is a key concept to understand protein function and biological processes related to protein functions. CoDNaS offers a well curated database that is experimentally driven, thoroughly linked, and annotated. CoDNaS facilitates the extraction of key information on small structural differences based on protein movements. CoDNaS enables users to easily relate the degree of conformational diversity with physical, chemical and biological properties derived from experiments on protein structure and biological characteristics. The new version of CoDNaS includes 70% of all available protein structures, and new tools have been added that run sequence searches, display structural flexibility profiles and allow users to browse the database for different structural classes. These tools facilitate the exploration of protein conformational diversity and its role in protein function. © The Author(s) 2016. Published by Oxford University Press.
format JOUR
author Monzon, A.M.
Rohr, C.O.
Fornasari, M.S.
Parisi, G.
author_facet Monzon, A.M.
Rohr, C.O.
Fornasari, M.S.
Parisi, G.
author_sort Monzon, A.M.
title CoDNaS 2.0: A comprehensive database of protein conformational diversity in the native state
title_short CoDNaS 2.0: A comprehensive database of protein conformational diversity in the native state
title_full CoDNaS 2.0: A comprehensive database of protein conformational diversity in the native state
title_fullStr CoDNaS 2.0: A comprehensive database of protein conformational diversity in the native state
title_full_unstemmed CoDNaS 2.0: A comprehensive database of protein conformational diversity in the native state
title_sort codnas 2.0: a comprehensive database of protein conformational diversity in the native state
url http://hdl.handle.net/20.500.12110/paper_17580463_v2016_n_p_Monzon
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AT fornasarims codnas20acomprehensivedatabaseofproteinconformationaldiversityinthenativestate
AT parisig codnas20acomprehensivedatabaseofproteinconformationaldiversityinthenativestate
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