TITLE:
A Method to Predict Amino Acids at Proximity of Beta-Sheet Axes from Protein Sequences
AUTHORS:
Antonin Guilloux, Bernard Caudron, Jean-Luc Jestin
KEYWORDS:
Polypeptide Chain; Protein Structure; Topology; Beta-Strand; Folding; Amino Acid; Structure Prediction
JOURNAL NAME:
Applied Mathematics,
Vol.5 No.1,
January
2,
2014
ABSTRACT: 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.