activity
20192026
collaborators

7 papers

q-bio.PE2026

Analyzing \b{eta}-Lactamase Evolution from the Principle of Least Action Perspective

Pablo Garay, Walter J. Lapadula, Maximiliano Juri Ayub +1

Protein sequences change over time due to the accumulation of mutations in the genes that encode them. Nonetheless, accurately identifying the most probable evolutionary pathways a…

q-bio.BM2026

Decoding How Proteins Fold

Jorge Vila

One of the most puzzling and unsolved challenges in molecular biology is understanding how proteins fold. Despite having advanced predictive tools that can accurately estimate the…

q-bio.PE2025

Factors controlling protein evolvability, at the molecular scale

Jorge A. Vila

This piece serves two purposes. Firstly, it aims at elucidating the role of epistasis in shaping, at a molecular level, the evolutionary paths of proteins, as well as the extent to…

q-bio.PE2024

Physical principles underpinning molecular-level protein evolution

J. A. Vila

Since protein mutations are the main driving force of evolution at the molecular level, a proper analysis of them (and the factors controlling them) will enable us to find a respon…

q-bio.PE2024

The Origin of Mutational Epistasis

Jorge A. Vila

The interconnected processes of protein folding, mutations, epistasis, and evolution have all been the subject of extensive analysis throughout the years due to their significance…

q-bio.BM2023

Analysis of proteins in the light of mutations

Jorge A. Vila

Proteins have evolved through mutations, amino acid substitutions, since life appeared on Earth, some 109 years ago. The study of these phenomena has been of particular significanc…

q-bio.BM2019

The Marginal Stability of Proteins: How Jiggling and Wiggling of Atoms are Connected to Neutral Evolution

Osvaldo A. Martin, Jorge A. Vila

Here we propose that the upper bound marginal stability of proteins (7.4 kcal/mol) is a universal property that includes macro-molecular complexes and is not affected by molecular…