The VizBiochem Lab
Powered by phone-camera magic © Dr. Panigrahi. All rights reserved.
Welcome
Our lab values equity, diversity, and inclusion and is committed to creating a fair and welcoming space for everyone interested in contributing to or learning from our research.
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We believe different perspectives make our research stronger and fuel innovation.
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Our goal is to remove barriers in science and support all team members, so everyone has the chance to succeed and contribute.
Research
Biomacromolecules including proteins, DNA, and RNA, are central to all biological processes. They encode genetic information, catalyze biochemical reactions, transmit signals, and provide structural scaffolding to the cells. Understanding their structure is essential for uncovering the macromolecular mechanisms that underpin life.
At the VizBiochem Lab, we investigate the structure and dynamics of biomacromolecules, with a focus on proteins and nucleic acids.
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Why proteins? Because they are the molecular machines that carry out the essential life functions, from metabolism to regulation.
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Why nucleic acids? DNA stores the genetic blueprint, while RNA serves as a versatile molecule for decoding, regulating, and sometimes catalyzing that information, which is central to gene expression and cellular identity.
Methodology
At the heart of our research is the idea that “seeing is believing”: by visualizing the molecules in action, we gain mechanistic insights that go far beyond what sequence or functional data alone can provide.
To explore these biomolecules in detail, we integrate advanced techniques:
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Cryo-electron microscopy (cryo-EM) for high-resolution structural snapshots
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Small-angle X-ray scattering (SAXS) for solution-state conformational analysis
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Molecular dynamics (MD) simulations to capture flexibility and conformational changes over time.
Through this research, we aim to uncover fundamental, unexplored principles of molecular structure and dynamics–bridging sequence data and biological insights in the post-genomic era.
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This knowledge is expected to inform our understanding of molecular evolution and advance insights into health and disease states.
Opportunities
We are assembling a team of curious minds, who get excited about by a crisp gel, feel the pure joy of a flawless PCR, live for the moment that stubborn protein finally purifies, and dream of solving macromolecular protein/nucleic acid structures.
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​If you have taken HuBi 2001 or related courses, are ambitious, experimentally fearless, and can pipette without looking (bonus if you actually do look), we want to hear from you! Please email your application, including an up-to-date CV, transcript, and the names of two referees to:
Dr. Panigrahi: rpanigrahi [AT] mun.ca
Bring your passion, your lab coat, your laptop, and maybe a backup USB drive.
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Honours projects and undergraduate research opportunities are available for motivated interns!
Gallery
Nucleosomes, the fundamental units of chromatin, interact with each other and with chromatin-binding factors to fold the genome into higher-order structures. Using cryo-EM, we have uncovered diverse nucleosomes stacking modes, including parallel arrangements (see video). When DNA unwraps from nucleosomes, it becomes susceptible to genotoxic stress and damage. Sensor proteins (pictured on the right) detect this damage and recruit kinases to phosphorylate specific histone sites, triggering the DNA damage response. Using cryo-EM and biophysical tools, we have shown how phosphorylated nucleosomes are selectively recognized by DNA repair factors.
©2025 by Dr. Panigrahi. All rights reserved.
Land Acknowledgement:
Memorial University campuses are situated in the traditional territories of Beothuk, Mi’kmaq, Innu, and Inuit people.
We acknowledge with respect the diverse histories and cultures of the Indigenous groups.
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