Cargando…
CalFitter 2.0: Leveraging the power of singular value decomposition to analyse protein thermostability
The importance of the quantitative description of protein unfolding and aggregation for the rational design of stability or understanding the molecular basis of protein misfolding diseases is well established. Protein thermostability is typically assessed by calorimetric or spectroscopic techniques...
Autores principales: | Kunka, Antonin, Lacko, David, Stourac, Jan, Damborsky, Jiri, Prokop, Zbynek, Mazurenko, Stanislav |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9252748/ https://www.ncbi.nlm.nih.gov/pubmed/35580052 http://dx.doi.org/10.1093/nar/gkac378 |
Ejemplares similares
-
CalFitter: a web server for analysis of protein thermal denaturation data
por: Mazurenko, Stanislav, et al.
Publicado: (2018) -
FireProt: web server for automated design of thermostable proteins
por: Musil, Milos, et al.
Publicado: (2017) -
EnzymeMiner: automated mining of soluble enzymes with diverse structures, catalytic properties and stabilities
por: Hon, Jiri, et al.
Publicado: (2020) -
HotSpot Wizard 3.0: web server for automated design of mutations and smart libraries based on sequence input information
por: Sumbalova, Lenka, et al.
Publicado: (2018) -
Exploration of Protein Unfolding by Modelling Calorimetry Data from Reheating
por: Mazurenko, Stanislav, et al.
Publicado: (2017)