A Method to Predict Amino Acids at Proximity of Beta-Sheet Axes from Protein Sequences

Autor:	Bernard Caudron, Antonin Guilloux, Jean-Luc Jestin
Rok vydání:	2014
Předmět:	Folding (chemistry) Quantitative Biology::Biomolecules Protein structure Beta sheet Phi value analysis Protein folding General Medicine Protein structure prediction Biological system Statistical potential Topology (chemistry) Mathematics
Zdroj:	Applied Mathematics. :79-89
ISSN:	2152-7393 2152-7385
DOI:	10.4236/am.2014.51009
Popis:	A general and elementary protein folding step was described in a previous article. Energy conservation during this folding step yielded an equation with remarkable solutions over the field of rational numbers. Sets of sequences optimized for folding were derived. In this work, a geometrical analysis of protein beta-sheet backbone structures allows the definition of positions of topological interest. They correspond to amino acids’ alpha carbons located on a unique axis crossing all beta-sheet’s strands or at proximity of this axis defined here. These positions of topological interest are shown to be highly correlated with the absence of sequences optimized for folding. Applications in protein structure prediction for the quality assessment of structural models are envisioned.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::e51b359ea05c807ecd02d9d0459d0a28 https://doi.org/10.4236/am.2014.51009 Zobrazit plný text záznamu