Physics
Martin Muschol
Martin Muschol
Assistant Professor
Contact
Office: PHY 0102A
Lab: PHY 102B/C
Phone: 813/974-2564
Email:
Links
Education
Ph.D. physics, 1992 City University of New York
Research
Research Interests:
- Imaging Neuronal Activity
- Modeling Neuronal Information Processing
- Protein Interactions, Aggregation and Phase Separation
- Colloidal Models of Protein Interactions
Short-Term Plastic Changes in Neurons: One fundamental property of neurons is their
"plasticity", i.e. their ability to alter their response after repeated stimulation. This ability is
thought to underlie such essential processes as learning and memory formation. We are using
high-speed optical recording techniques to monitor stimulation-induced changes in the spatial
and temporal patterns of electrical activity and calcium elevation in the axons innervating the
posterior pituitary gland. Using these optical data and simplified computational models, we are
trying to unravel how the regulation of excitable responses and of calcium dynamics contributes
to the well-known dependence of hormone release from the posterior pituitary gland on
stimulation pattern. More general, we hope to gain insights into the dynamic behavior of groups
of nerve cells and axons and how such dynamics contribute to neuronal plasticity.
Colloidal Models of Protein Aggregation: Proteins interact with each other either via nonspecific
physical interactions (Coulomb, van-der-Waals, hydrophobic) or via highly specific
interactions critical for their biological function. While most attention is focused on specific
interactions due to their importance to biological protein function, non-specific physical
interactions can play important roles, as well. Our lab is particularly interested how non-specific
interactions drive protein phase separation phenomena, including protein crystal growth, protein
precipitation, liquid-liquid phase separation and even amyloid fibril formation. We are using
spectroscopic techniques, light scattering, light microscopy and atomic force microscopy to
study protein phase separation phenomena and their relation to protein interactions.
Research Highlight
Transient Aggregates formed by Amyloid Proteins.
Atomic force microscope (AFM) images of small oligomers (two closely apposed structures in
front) and protofibrils (string of connected oligomers in the back) formed during the early stages
of amyloid fibril growth by hen egg white lysozyme. Amyloid proteins are related to many
devastating diseases, including Alzheimer's disease, Parkinson's disease and even type-2
diabetes. The AFM image is 125 nm on a side and the aggregates are 4 billionth of a meter (4nm)
tall.
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