Cargando…
Detection and sequence/structure mapping of biophysical constraints to protein variation in saturated mutational libraries and protein sequence alignments with a dedicated server
BACKGROUND: Protein variability can now be studied by measuring high-resolution tolerance-to-substitution maps and fitness landscapes in saturated mutational libraries. But these rich and expensive datasets are typically interpreted coarsely, restricting detailed analyses to positions of extremely h...
Autores principales: | Abriata, Luciano A., Bovigny, Christophe, Dal Peraro, Matteo |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4912743/ https://www.ncbi.nlm.nih.gov/pubmed/27315797 http://dx.doi.org/10.1186/s12859-016-1124-4 |
Ejemplares similares
-
Erratum to: Detection and sequence/structure mapping of biophysical constraints to protein variation in saturated mutational libraries and protein sequence alignments with a dedicated server
por: Abriata, Luciano A., et al.
Publicado: (2016) -
How Structural and Physicochemical Determinants Shape Sequence Constraints in a Functional Enzyme
por: Abriata, Luciano A., et al.
Publicado: (2015) -
Assessing the potential of atomistic molecular dynamics simulations to probe reversible protein-protein recognition and binding
por: Abriata, Luciano A., et al.
Publicado: (2015) -
Assessment of transferable forcefields for protein simulations attests improved description of disordered states and secondary structure propensities, and hints at multi-protein systems as the next challenge for optimization
por: Abriata, Luciano A., et al.
Publicado: (2021) -
PeSTo: parameter-free geometric deep learning for accurate prediction of protein binding interfaces
por: Krapp, Lucien F., et al.
Publicado: (2023)