Independent effects of protein core size and expression on residue-level structure-evolution relationships.
Recently, we demonstrated that yeast protein evolutionary rate at the level of individual amino acid residues scales linearly with degree of solvent accessibility. This residue-level structure-evolution relationship is sensitive to protein core size: surface residues from large-core proteins evolve...
Guardado en:
Autores principales: | Eric A Franzosa, Yu Xia |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2012
|
Materias: | |
Acceso en línea: | https://doaj.org/article/e43f365ec09d4ef09172321677dbf9d6 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Signatures of pleiotropy, economy and convergent evolution in a domain-resolved map of human-virus protein-protein interaction networks.
por: Sara Garamszegi, et al.
Publicado: (2013) -
Integrated assessment of genomic correlates of protein evolutionary rate.
por: Yu Xia, et al.
Publicado: (2009) -
The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core
por: Noah B. Bloch, et al.
Publicado: (2021) -
CopulaNet: Learning residue co-evolution directly from multiple sequence alignment for protein structure prediction
por: Fusong Ju, et al.
Publicado: (2021) -
Disentangling direct from indirect co-evolution of residues in protein alignments.
por: Lukas Burger, et al.
Publicado: (2010)