Using barcoded mutagenesis and a high-throughput genetic screen results in the identification of 150 genes that affect lipid accumulation in a non-model yeast system.
Complete mapping of human-adaptive mutations to the avian influenza PB2 protein shows how selection at key molecular interfaces combines with evolutionary accessibility to shape viral host adaptation.
The combination of computational modeling and protein design can reveal key determinants of antibody–antigen binding and optimize small sets of antigen variants for efficient experimental localization of epitopes.
Conventional studies have focused on enzymatic residues directly involved in catalysis; dissecting a potential interaction network within which these ‘catalytic residues’ are embedded provides insights fundamental to enzyme function, evolution, and engineering.
Deep mutational scanning was used to comprehensively quantify the effects of mutations to influenza hemagglutinin and shows that the virus possesses a high inherent mutational tolerance at key antigenic sites.
A generalizable approach to understanding the logic of molecular recognition reveals the contributions of individual residues to the specificity of protein-protein interactions.
Differing from its ortholog in Helicoverpa armigera, pheromone receptor HassOr14b is tuned to the major sex pheromone component in H. assulta, and two amino acids in the intracellular domain determine their ligand selectivity.
The extra dimensions in protein sequence space open up indirect paths of adaptation and alleviate the constraint on the selective accessibility to high fitness genotypes.
