Jeffrey M. Lotthammer

Direct prediction of intermolecular interactions driven by disordered regions

The paper develops a method to predict intermolecular interactions between intrinsically disordered regions and partner proteins using chemical physics principles.

Disentangling folding from energetic traps in simulations of disordered proteins

This paper introduces an algorithm to quantify local conformational heterogeneity in protein simulations, distinguishing between well-sampled, poorly-sampled, and folded regions of disordered proteins.

Accurate predictions of conformational ensembles of disordered proteins with STARLING

STARLING predicts conformational ensembles of disordered proteins from sequence, enabling rapid analysis of their structural plasticity and functional implications.

Complexes of vertebrate TMC1/2 and CIB2/3 proteins form hair-cell mechanotransduction cation channels

The paper shows that CIB2/3 and TMC1/2 form complexes essential for hair-cell mechanotransduction in vertebrates, supported by structural and functional analyses.

Metapredict enables accurate disorder prediction across the Tree of Life

Metapredict V3 predicts intrinsically disordered regions across 20,000 proteomes to assess disorder prevalence across life kingdoms.

High-throughput affinity measurements of direct interactions between activation domains and co-activators

This study quantifies direct interactions between 204 human activation domains and eight co-activators using a microfluidic platform, revealing 334 novel binding pairs and demonstrating the utility of analytical models for predicting activation.

Rhythmidia: a modern tool for circadian period analysis of filamentous fungi

Rhythmidia is a Python-based GUI tool for analyzing circadian periods and growth rates in Neurospora crassa race tube experiments, offering efficient and accurate results.

Protein Surface Chemistry Encodes an Adaptive Tolerance to Desiccation

The paper identifies protein surface chemistry as a determinant of desiccation tolerance and shows that modifying surface amino acids can confer tolerance to otherwise sensitive proteins.