
Anoop Arunagiri
Department of Biological Sciences, East Tennessee State University
Dr. Anoop Arunagiri is an assistant professor at the Department of Biological Sciences at East Tennessee State University. Holding a PhD in biophysics with extensive postdoctoral training in protein folding and metabolism, he brings a deep understanding of protein quality control to this collection. His laboratory’s primary research focuses on proinsulin proteostasis, investigating the molecular mechanisms of protein misfolding, aggregation, and endoplasmic reticulum (ER) stress in pancreatic beta cells, directly relevant to type 2 diabetes. Dr. Arunagiri is particularly interested in the crucial role of disulfide bonds in protein structure and oligomerization, and how these processes contribute to the formation of functional and pathological protein assemblies. His expertise spans various biochemical and cell biological approaches to characterize protein aggregation and its impact on cellular function.

Maria del Carmen Fernandez-Ramirez
UT Southwestern Medical Center
Dr. Maria del Carmen Fernandez-Ramirez, a postdoctoral researcher at UT Southwestern Medical Center, has over a decade of experience in the structural study of functional and pathological amyloid proteins. Her research aims to understand the structural features that dictate their folding and misfolding in relation to function and disease to identify targets for drug development. During her PhD, she investigated early stages of amyloidogenesis in intrinsically disordered proteins using AFM-based single-molecule force spectroscopy.Dr. Fernandez-Ramirez is currently studying the end stages of aggregation using cryo-electron microscopy to determine the structure of ex vivo fibrils in patients with systemic amyloidosis. Her research focuses on how specific mutations and tissue environments influence amyloid architecture, aiming to find potential connections between fibril structure and clinical manifestations. She has expertise in protein engineering and purification, ex vivo fibril extraction, and diverse biochemical and biophysical techniques for analyzing amyloid aggregation.

Sonja Kroschwald
ETH Zurich, 8092 Zurich, Switzerland
Dr. Sonja Kroschwald holds a Ph.D. in molecular biology with extensive postdoctoral training inbiochemistry and proteomics. She contributes a profound expertise in phase separation and proteinaggregation, exploring their roles in cellular physiology and pathology, to this collection. Herpublications focus on formation and regulation mechanisms of physiological protein condensates uponvarious triggers, as well as functional consequences of protein condensation for cell organization andcell function incl. metabolic changes. She also has a particular focus on understanding the processes thatgive rise to aberrant condensates, which are implicated in aging-related diseases such asneurodegeneration (e.g., Alzheimer's, Parkinson's, ALS) and cancer. Her expertise comprises structural,functional and biophysical protein characterization techniques, as well as proteomic and metabolomictechniques.
Protein self-assembly is a fundamental biological phenomenon that drives the formation of intricate cellular structures and, when dysregulated, contributes to the development of diseases such as diabetes, Alzheimer’s, and Parkinson’s. Understanding how proteins misfold, aggregate, and form biomolecular condensates is essential for unraveling disease mechanisms and advancing therapeutic innovation. This Methods Collection is designed to empower researchers with cutting-edge experimental and computational tools for precisely characterizing protein self-assembly. By assembling a comprehensive and accessible resource, we aim to accelerate discoveries into the molecular basis of protein aggregation disorders and the physiological functions of biomolecular condensates, ultimately paving the way for novel diagnostic and therapeutic strategies.
Production of hydrophobins and using thioflavin-T to monitor self-assembly
David Langelaan*1,
Isabela Drozdowski1,
Raymond He1
1Department of Biochemistry & Molecular Biology, Dalhousie University