Publication Details
Overview
 
 
Isel Grau, , Vranken, Wim
 

Contribution To Conference

Abstract 

Protein folding and function are closely connected, but the exact mechanisms by which proteins fold remain elusive. Early folding residues (EFRs) are amino acids within a particular protein that induce the very first stages of the folding process. High-resolution EFR data are only available for few proteins, which has previously enabled the training of a protein sequence-based machine learning black-box predictor (EFoldMine). Such a black-box approach does not allow a direct extraction of the early folding rules embedded in the protein sequence, whilst such interpretation is essential to improve our understanding of how the folding process works. We here apply and investigate a novel grey-box approach to the prediction of EFRs from protein sequence to gain mechanistic residue-level insights into the sequence determinants of EFRs in proteins. We interpret the rule set for three datasets, a default set comprised of natural proteins, a scrambled set comprised of the scrambled default set sequences, and a set of de novo designed proteins. Finally, we relate these data to the secondary structure adopted in the folded protein and provide all information online via http://xefoldmine.bio2byte.be/, as a resource to help understand and steer early protein folding.

Reference 
 
 
VUB