primary_duns:
824910376
cite this facility
Giselle Jacobson
The Biophysics Instrumentation Core (BIC) Facility offers sophisticated instrumentation dedicated to characterizing biomolecular conformations and interactions, as well as equipment for the isolation and purification of macromolecules for subsequent detailed biophysical analysis.
is_active:
Yesbudget_end:
05/14/2026date_added:
04/19/2025agency_code:
NIHfiscal_year:
2025project_num:
1S10OD038334-01award_amount:
$350,000.00budget_start:
05/15/2025org_name:
UNIVERSITY OF NOTRE DAMEorg_state:
INorg_country:
UNITED STATESorg_zipcode:
465565708primary_duns:
824910376abstract_text:
PROJECT SUMMARY Characterizing the sizes, shapes, and interactions of biomolecules is a crucial prerequisite to understanding biological function on a molecular level. Analytical ultracentrifugation (AUC) has been an essential component of the biophysical tool kit for decades, exploiting the distinct optical and sedimentation properties of proteins, nucleic acids, and polysaccharides to provide information on molecular structure and its changes. For example, changes in the stoichiometry of a multimeric protein caused by small molecule binding, or the addition of a partner protein, can be quickly and accurately quantified by changes in sedimentation properties. AUC measurements are made in a matrix-free solution, typically without the need for exogenous labels, more accurately capturing biological context than many other techniques commonly used to measure binding. AUC analysis does not destroy nor dilute precious samples, making them fully recoverable for additional downstream analyses. Over the past two decades, major advancements in AUC design now enable more rapid detection of more complex molecular assemblies using a large number of wavelengths for absorbance measurements. This proposal, in response to Program Announcement PAR-22-081, requests funds to purchase a state-of-the-art Beckman Coulter Optima A/I AUC to advance the research goals of University of Notre Dame’s NIH-funded scientists and engineers. This instrument will replace Notre Dame’s current Beckman Coulter ProteomeLab XL-I AUC, the only AUC broadly available within a 90-mile radius of Notre Dame. Despite careful maintenance and support over its lifetime at Notre Dame, the ProteomeLab AUC has been plagued by numerous malfunctions over the past year. Crucially, the ProteomeLab AUC will no longer be eligible for Beckman service support after 2025 and, at 18 years old, is optically and mechanically inadequate to modern instruments. The new AUC will be housed in a recently renovated and expanded core facility; its acquisition is an important piece of a large effort currently underway to expand and improve research infrastructure at the University of Notre Dame. As such, supervision, care, and maintenance of this instrument will contribute to employment stability for core facility staff, while access to this state-of-the-art research equipment will continue to grow the scope and scale of research at Notre Dame.project_title:
Beckman Optima A/I Analytical Ultracentrifuge (AUC)contact_pi_name:
MOBASHERY, SHAHRIARtotal_cost:
$349,999.00total_cost:
$1.00is_active:
Nobudget_end:
05/14/2025date_added:
05/18/2024agency_code:
NIHfiscal_year:
2024project_num:
1S10OD036273-01award_amount:
$106,804.00budget_start:
05/15/2024org_name:
UNIVERSITY OF NOTRE DAMEorg_state:
INorg_country:
UNITED STATESorg_zipcode:
465565708primary_duns:
824910376abstract_text:
PROJECT SUMMARY Characterization of protein conformational changes is a crucial prerequisite to understanding biological functions on a molecular level. Circular dichroism (CD) spectroscopy has been an essential component of the biophysical tool kit for decades, exploiting the chiral properties of small molecules, proteins, and nucleic acids to provide information on molecular structure and its changes. For example, changes in secondary structure caused by protein unfolding (induced by perturbants such as temperature or pH), or folding (induced by the binding of a small molecule ligand, protein, or nucleic acid) can be quickly and easily quantified as changes in the far-UV CD spectrum. Separately, CD spectroscopy is also an essential technique in the study of chiral- selective properties of small molecules, including drugs, fluorescent dyes, and chemical catalysts designed to mimic enzymatic catalysis. Over the past decade, advancements in instrument optics and nitrogen purging, as well as the development of additional functionalities such as simultaneous fluorescence and absorbance detection, have further enhanced the utility of CD spectroscopy for biomedical studies. This proposal, in response to Program Announcement PAR-22-081, requests funds to purchase a state-of-the-art Jasco J-1500 CD spectropolarimeter to advance the research goals of University of Notre Dame scientists. This instrument will replace Notre Dame’s current Jasco J-815 instrument, which although still productive and carefully maintained for its >13-year lifespan, is optically inferior to modern instruments and operated by an obsolete computer. The new instrument will be housed in a recently renovated and expanded core facility; its acquisition is an important piece of a large effort currently underway to expand and improve research infrastructure at the University of Notre Dame. As such, supervision, care, and maintenance of this instrument will contribute to employment stability for core facility staff, while access to this state-of-the-art research equipment will continue to grow the research enterprise at Notre Dame.project_title:
Upgraded circular dichroism spectropolarimeter for Notre Dame Biophysics Instrumentation Core Facilitycontact_pi_name:
CLARK, PATRICIA LOUISEtotal_cost:
$106,804.00is_active:
Nobudget_end:
07/09/2021date_added:
07/11/2020agency_code:
NIHfiscal_year:
2020project_num:
1S10OD028553-01award_amount:
$342,782.00budget_start:
07/10/2020org_name:
UNIVERSITY OF NOTRE DAMEorg_state:
INorg_country:
UNITED STATESorg_zipcode:
465565708primary_duns:
824910376abstract_text:
PROJECT SUMMARY Characterization of biomolecular interactions is a crucial pre-requisite to understanding biological functions on a molecular level. Surface plasmon resonance (SPR) has been an essential component of the biophysical tool kit for decades, providing fundamental information about the interactions between various types of biomolecules, including information about kinetics, affinities, specificity, and underlying thermodynamic quantities. Currently, a state-of-the-art SPR instrument is not broadly available to University of Notre Dame researchers. In response to Program Announcement PAR-19-179, this proposal requests funds to purchase a Biacore T200 SPR system to further the research goals of Notre Dame scientists. The NIH-funded researchers will use the T200 for a variety of projects, including understanding and improving specificity in cellular immunity, characterizing the bacterial cell wall degradome, characterize the interaction of pathogenic bacteria with host cells and designing small molecule inhibitors of molecular chaperones with anti-cancer and neuroprotective effects. This instrument will fulfill an urgent need for access to a shared SPR instrument at Notre Dame. To ensure broad access, the new instrument will be housed in the centrally-located, newly established Biophysics Instrumentation Core (BIC) Facility, where new user training, general operations and upkeep will be overseen by a PhD-level staff scientist. The proposed instrument represents one piece of a large effort currently underway to expand and improve research infrastructure at Notre Dame.project_title:
BIACORE T200 SPR FOR NOTRE DAME BIOPHYSICS INSTRUMENTATION CORE (BIC) FACILITYcontact_pi_name:
BAKER, BRIAN Mtotal_cost:
$342,782.00Services are offerred outside of
Consulting is offerred outside of University of Notre Dame
Last Updated: 04/29/2026
