ThermoMutDB: a thermodynamic database for missense mutations

Proteins are intricate, dynamic structures, and small changes in their amino acid sequences can lead to large effects on their folding, stability and dynamics. To facilitate the further development and evaluation of methods to predict these changes, we have developed ThermoMutDB, a manually curated...

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Detalles Bibliográficos
Autores principales: Xavier, Joicymara S, Nguyen, Thanh-Binh, Karmarkar, Malancha, Portelli, Stephanie, Rezende, Pâmela M, Velloso, João P L, Ascher, David B, Pires, Douglas E V
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2020
Materias:
Database Issue
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7778973/
https://www.ncbi.nlm.nih.gov/pubmed/33095862
http://dx.doi.org/10.1093/nar/gkaa925

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7778973/
https://www.ncbi.nlm.nih.gov/pubmed/33095862
http://dx.doi.org/10.1093/nar/gkaa925

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