Proteins evolvability upon point mutations
Year: 2021
Type: preprint
Abstract: The primary aim of this work is to explore how proteins point mutations impact their marginal stability and, hence, their evolvability. With this purpose is shown that the use of four classic notions, namely, those from Leibniz & Kant (1768), Maynard Smith (1970), Einstein & Infeld (1961), and Anfinsen (1973), are sufficient to understand the origin of the main factor controlling the protein evolvability. The preliminary results -- without considering epistasis effects explicitly -- indicate that the protein marginal-stability change upon point mutations provides the necessary and sufficient information to describe, through a Boltzmann factor, the evolution of the amide hydrogen-exchange protection factors. This finding is of paramount importance because it illustrates the impact of point mutations on both the protein marginal-stability and the ensemble of folded conformations coexisting with the native state and, in the presence of metamorphism, on the propensity for the appearance of new folds and functions.
Source: arXiv (Cornell University)
Author: Jorge A. Vila
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W3213128975