TY - JOUR
T1 - Mutational Paths with Sequence-Based Models of Proteins
T2 - From Sampling to Mean-Field Characterization
AU - Mauri, Eugenio
AU - Cocco, Simona
AU - Monasson, Rémi
N1 - Publisher Copyright:
© 2023 American Physical Society.
PY - 2023/4/14
Y1 - 2023/4/14
N2 - Identifying and characterizing mutational paths is an important issue in evolutionary biology, with potential applications to bioengineering. We here propose an algorithm to sample mutational paths, which we benchmark on exactly solvable models of proteins in silico, and apply to data-driven models of natural proteins learned from sequence data with restricted Boltzmann machines. We then use mean-field theory to characterize paths for different mutational dynamics of interest, and to extend Kimura's estimate of evolutionary distances to sequence-based epistatic models of selection.
AB - Identifying and characterizing mutational paths is an important issue in evolutionary biology, with potential applications to bioengineering. We here propose an algorithm to sample mutational paths, which we benchmark on exactly solvable models of proteins in silico, and apply to data-driven models of natural proteins learned from sequence data with restricted Boltzmann machines. We then use mean-field theory to characterize paths for different mutational dynamics of interest, and to extend Kimura's estimate of evolutionary distances to sequence-based epistatic models of selection.
U2 - 10.1103/PhysRevLett.130.158402
DO - 10.1103/PhysRevLett.130.158402
M3 - Article
C2 - 37115874
AN - SCOPUS:85153084649
SN - 0031-9007
VL - 130
JO - Physical Review Letters
JF - Physical Review Letters
IS - 15
M1 - 158402
ER -