A copy of this work was available on the public web and has been preserved in the Wayback Machine. The capture dates from 2022; you can also visit the original URL.
The file type is application/pdf
.
Atomistic simulation of protein evolution reveals sequence covariation and time-dependent fluctuations of site-specific substitution rates
[article]
2022
bioRxiv
pre-print
AbstractThermodynamic stability is a crucial fitness constraint in protein evolution and is a central factor in shaping the sequence landscapes of proteins. The correlation between stability and molecular fitness depends on the mechanism that relates the biophysical property with biological function. In the simplest case, stability and fitness are related by the amount of folded protein. However, when proteins are toxic in the unfolded state, the fitness function shifts, resulting in higher
doi:10.1101/2022.06.01.494278
fatcat:mj7tmdzgbbf7pmhfsvvcyyyjgq