Alexander Kai Buell

This study benchmarks DSF across labs, showing variability in thermal stability parameters due to instruments, workflows, and fluorescence readouts, with harmonization and centralized analysis improving consistency.

The paper introduces a method to resolve energy differences in heterogeneous protein complexes using cryo-EM data and applies it to study cruciferin isoforms.

This study uses systematic K-to-Q mutagenesis to probe the energy landscape of α-Synuclein aggregation, identifying core residue mutations that alter free energy pathways and fibril polymorphism.

The paper shows RNA modulates assembly and activity of two -helical peptides, PSM3 and LL-37, through phase separation and aggregation dynamics, affecting virulence and host defense.

This study develops a high-throughput method to quantify interactions driving condensate formation in intrinsically disordered proteins and shows amino acid content primarily determines partitioning behavior.

This study shows that terminal truncations of α-synuclein significantly alter phase separation, while familial mutations have minimal effects, influencing amyloid fibril formation and condensate behavior.

This study designs polymorph-specific binders for α-synuclein fibrils using a computational pipeline, demonstrating their utility as selective labeling agents without interfering with fibril dynamics.

This study shows that the thermodynamic stability of alpha-synuclein fibrils affects their disaggregation by the chaperone system HSP70, DNAJB1, and Apg2, with more stable fibrils being less efficiently disaggregated.

The paper shows that different structures of alpha-synuclein fibrils affect how Hsc70 chaperones disaggregate them, influencing protein quality control and aggregation.

This paper enhances fluorinase catalytic efficiency by engineering mutants and optimizing reaction conditions, achieving a 60-fold increase in turnover rate.

This paper develops a global kinetic model of lipid-induced alpha-synuclein aggregation and identifies how squalamine inhibits this process by reducing lipid-dependent primary nucleation.