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Simple approach for ranking structure determining residues
OSCAR DANIEL LUNA MARTINEZ
ABRAHAM MARCELINO VIDAL LIMON
MIRYAM IVETTE VILLALBA VELAZQUEZ
RAMON GARDUÑO JUAREZ
Vladimir Uversky
BALTAZAR BECERRIL LUJAN
Acceso Abierto
Atribución-NoComercial-SinDerivadas
https://doi.org/10.7717/peerj.2136
Molecular dynamics
Shannon dynamical entropy
Intrinsic disorder
Thermodynamics
"Mutating residues has been a common task in order to study structural properties of the protein of interest. Here, we propose and validate a simple method that allows the identification of structural determinants; i.e., residues essential for preservation of the stability of global structure, regardless of the protein topology. This method evaluates all of the residues in a 3D structure of a given globular protein by ranking them according to their connectivity and movement restrictions without topology constraints. Our results matched up with sequence-based predictors that look up for intrinsically disordered segments, suggesting that protein disorder can also be described with the proposed methodology."
PeerJ, Inc
2016-06
Artículo
Luna-Martínez OD, Vidal-Limón A, Villalba-Velázquez MI, Sánchez-Alcalá R, Garduño-Juárez R, Uversky VN, Becerril B. (2016) Simple approach for ranking structure determining residues. PeerJ 4:e2136 https://doi.org/10.7717/peerj.2136
BIOLOGÍA MOLECULAR
Versión publicada
publishedVersion - Versión publicada
Aparece en las colecciones: Publicaciones Científicas Biología Molecular

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