• Publications
  • Influence
Why highly expressed proteins evolve slowly.
TLDR
It is hypothesized that selection to reduce the burden of protein misfolding will favor protein sequences with increased robustness to translational missense errors, and genome-wide tests favor the translational robustness explanation over existing hypotheses that invoke constraints on function or translational efficiency.
Deep mutational scanning of SARS-CoV-2 receptor binding domain reveals constraints on folding and ACE2 binding
TLDR
An interactive visualization and open analysis pipeline is presented to facilitate use of the dataset for vaccine design and functional annotation of mutations observed during viral surveillance.
Protein stability promotes evolvability.
TLDR
This work uses simulations with model lattice proteins to demonstrate how extra stability increases evolvability by allowing a protein to accept a wider range of beneficial mutations while still folding to its native structure.
Permissive Secondary Mutations Enable the Evolution of Influenza Oseltamivir Resistance
TLDR
It is shown that H274Y decreases the amount of neuraminidase that reaches the cell surface and that this defect can be counteracted by secondary mutations that also restore viral fitness.
Complete mapping of mutations to the SARS-CoV-2 spike receptor-binding domain that escape antibody recognition
TLDR
A deep mutational scanning method is described to map how all amino-acid mutations in the RBD affect antibody binding, and a complete escape-mutation maps enable rational design of antibody therapeutics and assessment of the antigenic consequences of viral evolution.
Protocol and reagents for pseudotyping lentiviral particles with SARS-CoV-2 Spike protein for neutralization assays
TLDR
It is demonstrated how these pseudotyped lentiviral particles can be used to measure the neutralizing activity of human sera or plasma against SARS-CoV-2 in convenient luciferase-based assays, thereby providing a valuable complement to ELISA-based methods that measure antibody binding rather than neutralization.
Thermodynamic prediction of protein neutrality.
TLDR
A simple theory that uses thermodynamic parameters to predict the probability that a protein retains the wild-type structure after one or more random amino acid substitutions is presented and provides a basis for interpreting the response of proteins to substitutions in protein engineering applications.
Stability-mediated epistasis constrains the evolution of an influenza protein
TLDR
This work created all intermediates along a 39-mutation evolutionary trajectory of influenza nucleoprotein, and introduced each mutation individually into the parent, painting a coherent portrait of epistasis during nucleop protein evolution.
Structural determinants of the rate of protein evolution in yeast.
TLDR
Evidence is provided that protein structure plays an important role in shaping the rate of sequence evolution and evidence to support recent theoretical advances linking structural designability to contact density is provided.
...
1
2
3
4
5
...