K. E. Johansson

The paper identifies 5 stabilizing mutations for PYR1 variants using GMMA that increase thermal stability without affecting functionality across different ligand-binding capabilities.

This study maps Parkin missense variants' abundance and degradation mechanisms, showing most low-abundance variants are degraded via the ubiquitin-proteasome system and stabilized at lower temperatures.

The paper develops a model to predict conformational ensembles of human intrinsically disordered regions (IDRs) from sequence, showing correlations between chain compaction, function, localization, and sequence conservation across orthologs.

This paper introduces RaSP, a deep learning method for rapid protein stability prediction, showing it matches biophysics-based methods and reveals population-level patterns in stability changes.

The paper uses a computational model to infer substitution effects from high-throughput experiments, increasing protein stability through targeted amino acid changes.

The paper identifies conserved degron features in yeast, viruses, and humans that govern quality control proteolysis, showing transmembrane domain-like sequences are key determinants of protein half-life.

The paper shows that Hsp70-binding motifs can function as PQC degrons, targeting misfolded proteins for degradation in yeast and human cells.

The paper assesses computational protein design templates using Rosetta Design and experimental validation, finding that the cart_bonded energy term improves template selection for successful designs.

This paper introduces GMMA, a method to identify beneficial amino acid substitutions in proteins using multi-mutant data, and applies it to GFP variants to find stabilizing and functional improvements.

The paper analyzes variant effects on protein activity and abundance in NUDT15 and PTEN, finding that a third of variants cause loss of function and half of these also reduce abundance.

This study investigates charge interactions in a charge-depleted protein using simulations and experiments, revealing context-dependent residue interactions and their impact on protein stability.

This paper introduces a method to assess protein stability using combined temperature and denaturant unfolding with minimal protein requirements, demonstrating its applicability for small-scale protein purification.