Document Type
Article
Publication Date
2016
Keywords
Molecular dynamics, Shannon dynamical entropy, Intrinsic disorder, Thermodynamics
Digital Object Identifier (DOI)
https://doi.org/10.7717/peerj.2136
Abstract
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.
Rights Information
This work is licensed under a Creative Commons Attribution 4.0 License.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
PeerJ, v. 4, art. e2136
Scholar Commons Citation
Luna-Martínez, Oscar D.; Vidal-Limón, Abraham; Villalba-Velázquez, Miryam I.; Sánchez-Alcalá, Rosalba; Garduño-Juárez, Ramón; Uversky, Vladimir N.; and Becerril, Baltazar, "Simple Approach for Ranking Structure Determining Residues" (2016). Molecular Medicine Faculty Publications. 1.
https://digitalcommons.usf.edu/mme_facpub/1
