Characterizing Intermolecular Interactions That Initiate Native-Like Protein Aggregation

Characterizing Protein-Protein interactions by iTC

Proteins operate as integral members of complex networks that precisely regulate physiological processes through a combination of signaling pathways and feedback. These regulatory functions, including signal transduction, protein trafficking, transcription and translation, all rely on the ability of proteins to rapidly target and form specific non-covalent complexes with other proteins in respo...

Tau protein liquid–liquid phase separation can initiate tau aggregation

The transition between soluble intrinsically disordered tau protein and aggregated tau in neurofibrillary tangles in Alzheimer's disease is unknown. Here, we propose that soluble tau species can undergo liquid-liquid phase separation (LLPS) under cellular conditions and that phase-separated tau droplets can serve as an intermediate toward tau aggregate formation. We demonstrate that phosphoryla...

Intermolecular Interactions The Ig-Like Domain of Tapasin Influences

Intermolecular Interactions and Protein Dynamics by Solid‐State NMR Spectroscopy

Understanding the dynamics of interacting proteins is a crucial step toward describing many biophysical processes. Here we investigate the backbone dynamics for protein GB1 in two different assemblies: crystalline GB1 and the precipitated GB1-antibody complex with a molecular weight of more than 300 kDa. We perform these measurements on samples containing as little as eight nanomoles of GB1. Fr...

Characterizing Cyclin J By Identifying Conserved Protein-Protein Interactions

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