Comprehensive analyses of how mutations in a picornavirus capsid affect viral fitness provide novel insights into viral biology, evolution, and host interactions.

Yeast populations lose mutational robustness during evolution in one environment but not in another due to the collective effect of a large number of idiosyncratic epistatic interactions.

Environmental conditions strongly impact the fitness effects of Hsp90, resulting in the selection of Hsp90 sequences in nature that are robust to a variety of stressful conditions.

A combination of genetics, experimental evolution and mathematical modelling defines information necessary to predict the outcome of short-term adaptive evolution.

A new model describes how adaptive molecular evolution shapes phylogenetic trees and can be used to estimate the fitness effects of mutations from phylogenies.

Chemical perturbation-dependent deep mutational scanning data collected by a lab-based interdisciplinary graduate class resolves a paradox between the high evolution conservation and the high mutational tolerance of the protein ubiquitin.

By measuring the impacts of thousands of mutations on potassium channel trafficking and function, we illuminate the molecular basis of folding, structure–function relationships, and how these are altered in disease.

Pleiotropy of adaptive clones isolated from diverse experimental environment.

Some of the mutations that occur during influenza evolution can only be tolerated in conjunction with other mutations that increase the stability of a viral protein.

Changes to cellular protein homeostasis reveal widespread advantageous effects of destabilizing mutations, opening the possibility to switch mutational landscapes back-and-forth from permissive to restrictive.