Protein Folding from the Perspective of Chaperone Action
Abstract
Predicting the three-dimensional (3D) functional structures of proteins remains an important computational milestone in molecular biology to be achieved. This feat is hinged on a clear understanding of the mechanism which proteins use to fold into their native structures. Since Levinthal's paradox, there has been a lot of progress in understanding this mechanism. Most of the earlier attempts were caught between assigning either hydrophobic interactions or hydrogen bonding as the dominant folding force. However, a consensus now seems to be emerging about hydrogen bonding being a stronger force. Interestingly, a view from chaperone action may further throw some light on the nature of the folding mechanism. Thus the very mechanisms which prevent protein aggregation and misfolding, could help us have a better understanding of the folding mechanism itself.
Keywords
Cite
@article{arxiv.1911.11900,
title = {Protein Folding from the Perspective of Chaperone Action},
author = {Samuel Nkrumah},
journal= {arXiv preprint arXiv:1911.11900},
year = {2019}
}