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Tatyana Polenova uses UD's Nuclear Magnetic Resonance (NMR) Laboratory to analyze the structures of viruses and biological assemblies at an atomic level, to better understand their role in disease.
In her continuing
search for clues to understanding structural biology underlying disease,
University of Delaware chemist Tatyana Polenova analyzes, atom by atom,
the structure of viruses and biological assemblies.
In order to see and examine those systems, she makes use of UDs Nuclear Magnetic Resonance (NMR) Laboratory.
The two-story space in Brown Lab houses an array of large instruments
that offer scientists an atomic-level view of the structures, dynamics
and functions of complex molecular assemblies.
A biophysical chemist and professor of chemistry and biochemistry,
Polenova has led research teams in making important breakthroughs in a
number of areas. These include new discoveries about the structure of
the HIV virus and about proteins binding with microtubules, the
latticework of tiny tubes in human cells whose malfunction can lead to
Her research relies on NMR spectroscopy, which is a powerful and
versatile tool that uses the magnetic properties of atomic nuclei to
analyze the structure of a wide variety of materials. It enables
scientists to identify every atom in a structure and to see how each
Its a technique that is essential, Polenova says, not only for her
own lab but for many scientists who are seeking to understand large
NMR spectroscopy has found applications in chemistry, biochemistry,
physics and medicine, she said. Its often used with the discovery of
new substances, to get an atomic-level fingerprint of the material,
and pharmaceutical companies use it to analyze how compounds can be
Now, her work in the field of physical biochemistry has been
recognized by the International Society of Magnetic Resonance, which has
named her one of four new Fellows of the organization.
Her election by the societys other Fellows is a tribute to your
many contributions in the field of magnetic resonance, including both
your world-leading research activities and your support of the magnetic
resonance community, the organizations president, Robert Tycko, wrote
in notifying Polenova of the honor.
The society elects a maximum of four new Fellows a year to join a
very distinguished international group of outstanding scientists,
spanning several generations and encompassing many areas of research,
Move this whole section up, swapping places with the section above it.
To prepare for analyzing a sample, Tatyana Polenova
adjusts the cables beneath the nuclear magnetic resonance instrument.
Its like tuning a radio, she says. You need to find the right
The field of magnetic resonance includes a range of research
methods, such as nuclear magnetic resonance (NMR) and electron
paramagnetic resonance (EPR) spectroscopy, as well as magnetic resonance
imaging (MRI). The various methods are critical research tools in
fields including physics, chemistry, life sciences, materials research
My research is focused on large systems, which are much more
complicated than small molecules, Polenova said. It requires very
special approaches and equipment to learn the details of the structure
and dynamics, to the atomic resolution.
Some of her published research has provided new insights into the HIV
capsid, which is the protein shell that encloses the virus that causes
AIDS. Learning more about how the capsid develops and its role in the
infection process has provided investigators with important information.
Understanding the structural biology of HIV gives us clues that we
hope might be a possible step toward treatment, Polenova said.
Her research also focuses on microtubules, which carry essential
proteins in our cells. In a 2015 publication in Proceedings of the
National Academy of Sciences, her team reported the first-ever
atomic-resolution view of one of these proteins bound to a microtubule.
The finding provides critical insights into the way mutations in certain proteins cause neurological and degenerative disorders.
Her teams microtubule and HIV protein assemblies analysis was made
through the use of an NMR technique called magic-angle spinning. A
sample is placed in a tube in the NMR instrument, which spins it inside
the NMR magnet at the precise angle needed to generate atomic-resolution
data about the samples structure.
When you put the sample in, you can adjust the angle slightly, and
you adjust the temperature, Polenova said. When it spins, you can
observe every atom in the molecule. Its like driving a car, and youre
in the drivers seat.
Polenova, who earned her doctorate and conducted postdoctoral
research at Columbia University, joined the UD faculty in 2003. Since
2014, she has been director of the National Institutes of Healths
Center of Biomedical Research Excellence (COBRE) Molecular Design of
Advanced Biomaterials program at UD.
Article by Ann Manser; photos by Kathy F. Atkinson