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Piotr E. Marszalek

Professor in the Thomas Lord Department of Mechanical Engineering and Materials Science
Thomas Lord Department of Mechanical Engineering and Materials Science
3387 FCIEMAS Building, Box 90300, Durham, NC 27708-0300
3387 FCIEMAS Building, Box 90300, Durham, NC 27708

Overview


My research focuses on investigating relationships between structural and mechanical properties of biopolymers (polysaccharides, DNA, proteins), which I study at a single molecule level. My main approaches are experimental scanning probe microscopy techniques and computational methods involving Molecular Dynamics simulations and ab initio quantum mechanical calculations. The ultimate goal of this research is to understand the above-mentioned relationships at an atomic level and to apply the knowledge gained towards elucidating basic phenomena such as: molecular recognition that mediates interactions between proteins and sugars, mechanotransduction that underlies mechanical sensing and hearing in all organisms, and protein folding that is fundamental to all biology. Our DNA research is aimed at exploiting atomic force microscopy techniques to develop new ultra-sensitive assays for detecting and examining DNA damage, the process underlying carcinogenesis, and to increase our mechanistic understanding of DNA damage and repair processes. This research, in addition to its basic science aspects will lay a foundation for the future use of AFM technologies in the nanoscale DNA diagnostics with a potential to directly benefit human health.

Current Appointments & Affiliations


Professor in the Thomas Lord Department of Mechanical Engineering and Materials Science · 2009 - Present Thomas Lord Department of Mechanical Engineering and Materials Science, Pratt School of Engineering

In the News


Published January 17, 2020
Learning How Molecules Function by Stretching and Tearing Them Apart

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Recent Publications


Nanoluc oligoproteins as a model system for protein misfolding and refolding studies.

Journal Article Biophysical journal · December 2025 Protein misfolding can lead to protein malfunction, which may compromise cell viability. Chaperones, including the HSP70 system, are proteins that have evolved to restore the native structure of misfolded proteins. Although most chaperones, including DnaK ... Full text Cite

Denaturation of firefly luciferase at heat shock temperatures captured in silico.

Journal Article Biophysical journal · August 2025 Firefly luciferase (Fluc) is a bioluminescent protein that is widely used in cell and molecular biology research. Specifically, it is a gold standard substrate in chaperone protein studies because its bioluminescence decrease and recovery are related to Fl ... Full text Cite

Tandem repeats of highly bioluminescent NanoLuc are refolded noncanonically by the Hsp70 machinery.

Journal Article Protein science : a publication of the Protein Society · February 2024 Chaperones are a large family of proteins crucial for maintaining cellular protein homeostasis. One such chaperone is the 70 kDa heat shock protein (Hsp70), which plays a crucial role in protein (re)folding, stability, functionality, and translocation. Whi ... Full text Cite
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Recent Grants


University Training Program in Biomolecular and Tissue Engineering

Inst. Training Prgm or CMEMentor · Awarded by National Institute of General Medical Sciences · 1994 - 2027

Transition to Excellence: From Single-Molecule Force Spectroscopy to Single-Particle Cryogenic Electron Microscopy

ResearchPrincipal Investigator · Awarded by National Science Foundation · 2021 - 2025

EAGER: Exploring the Quantum-Mechanical Basis of Odorant Detection by Olfactory Receptors

ResearchPrincipal Investigator · Awarded by National Science Foundation · 2021 - 2024

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Education, Training & Certifications


Electrotechnical Institute (Poland) · 1991 Ph.D.
University of Warsaw (Poland) · 1985 M.S.

External Links


Marszalek Lab