D. Tullman-Ercek

Characterization and Engineering of the Type 3 Secretion System Needle Monomer from Salmonella Through the Construction and Screening of a Comprehensive Mutagenesis Library

This paper constructs and screens a mutagenesis library of the PrgI protein to identify mutations that enhance T3SS secretion titer and establish design rules for engineering the secretion system.

Systematic Engineering of Virus-Like Particles to Identify Self-Assembly Rules for Shifting Particle Size

The paper systematically engineers virus-like particles to identify self-assembly rules that control particle size by mutating key residues in coat proteins and analyzing the effects.

Comprehensive Fitness Landscape of a Multi-Geometry Protein Capsid Informs Machine Learning Models of Assembly

The paper generates fitness landscapes for two VLP capsid geometries and uses them to train machine learning models for predicting mutational effects on assembly.

Vertex protein PduN tunes encapsulated pathway performance by dictating bacterial metabolosome morphology

The paper investigates how removing the vertex protein PduN alters the morphology of the Pdu MCP microcompartment in Salmonella, affecting pathway performance through changes in surface area to volume ratios.

Computational and experimental approaches to controlling bacterial microcompartment assembly

The paper uses computational and experimental methods to control bacterial microcompartment assembly by modifying protein interactions and angles.

Self-assembling shell proteins PduA and PduJ have essential and redundant roles in bacterial microcompartment assembly

The paper investigates the roles of PduA and PduJ in bacterial microcompartment assembly, showing they are essential and redundant, with no compensation from other proteins.

Engineering a virus-like particle to display peptide insertions using an apparent fitness landscape

The paper engineers MS2 virus-like particles with peptide insertions using SyMAPS to map insertion effects on capsid assembly and function.