Jonathan Dinman to Direct the Institute for Bioscience and Biotechnology Research
Jonathan Dinman, a professor in the Department of Cell Biology and Molecular Genetics at the University of Maryland, College Park (UMCP), has been named director of the Institute for Bioscience and Biotechnology Research (IBBR), effective November 1, 2024. Located in the heart of Maryland’s biotechnology corridor in Montgomery County, IBBR...
Breakthrough Rapid Detection Method for Monoclonal Antibody Redox Modifications Published in Nature Chemical Biology
Monoclonal antibodies (mAbs) represent the largest class of the growing therapeutic protein market. The structure and function, and therefore the safety and efficacy, of these molecules can be affected by reduction-oxidation (redox)-based chemical modifications such as interchain disulfide bond reduction and methionine oxidation. In manufacturing, new analytical technologies are needed...
IBBR Researchers Participate in NIH Established Pandemic Preparedness Research Network
The University of Maryland Institute for Bioscience and Biotechnology Research (IBBR) received a $2.95M grant subaward from the National Institute of Allergy and Infectious Diseases (NIAID), part of the National Institutes of Health (NIH) to conduct cutting-edge research aimed at developing vaccines and monoclonal antibodies (mAbs) to combat high-priority viral...
About IBBR
IBBR is a joint research enterprise of the University of Maryland, College Park, the University of Maryland, Baltimore, and the National Institute of Standards and Technology.
IBBR leverages state-of-art integrative methods for bioanalytical, biophysical and structural characterization of biomolecules: cryo-electron microscopy, nuclear magnetic resonance, x-ray crystallography, small angle neutron and x-ray scattering and mass spectrometry.
IBBR researchers seek to advance therapeutic development, biomanufacturing, and state-of-the-art measurement technologies, to support accelerated delivery of safe and effective medicines to the public.
IBBR is a major initiative and supported in part by the University of Maryland Strategic Partnership: MPowering the State (MPower) , an initiative designed to achieve innovation and impact through collaboration.
Connecting
IBBR Commons
Sophisticated state-of-the-art instrumentation and facilities, and in-house expertise located in shared space and dedicated to advance research, support collaboration and foster innovation of methods. Instrumentation and facilities include tools for high-resolution structural biology, bioanalytical and biophysical measurement, protein engineering and cell culture, advanced computation including artificial intelligence and deep learning methods, and general laboratory services. These capabilities and advanced training are available to IBBR scientists and collaborators.
IBBR Postdoc Program
The IBBR Postdoc Program (IPP) focuses on collaborative research involving basic science and technology development that advances therapeutic development, vaccine development, and biomanufacturing. IPP Fellow project teams are designed with a combination of the IPP Fellow career goals and priorities of project mentors who can be from academic, government, and/or industrial laboratories throughout the University of Maryland, NIST and the I-270 corridor.
NMRPipe
IBBR is home to NMRPipe, a popular collection of programs and scripts for manipulating multidimensional Nuclear Magnetic Resonance (NMR) data. The use of NMRPipe is noted in roughly 40% of all NMR structures accepted into the Protein Data Bank.
Upcoming Events
NIST Group Meeting; Vamsi Bolla
Wednesday, January 8, 2025 - 11:00am
BMD Staff Seminar E. Erisman/ M. Lowenthal, .04/.08
E. Erisman/ M. Lowenthal, .04/.08
Tuesday, January 14, 2025 - 11:00am
NIST Group Meeting, Anupreet Kaur
Wednesday, January 15, 2025 - 11:00am
Recent Publications
Recognition of Self and Viral Ligands by NK Cell Receptors.
Natural killer (NK) cells are essential elements of the innate immune response against tumors and viral infections. NK cell activation is governed by NK cell receptors that recognize both cellular...
Detection of Putative Ligand Dissociation Pathways in Proteins Using Site-Identification by Ligand Competitive Saturation.
Drug efficacy often correlates better with dissociation kinetics than binding affinity alone. To study binding kinetics computationally, it is necessary to identify all of the possible ligand...
Rapid Removal of IgG1 Carryover on Protease Column Using Protease-Safe Wash Solutions Delivered with LC Pump for HDX-MS Systems.
Sample carryover is a common problem in hydrogen-deuterium exchange mass spectrometry, particularly because immobilized protease columns cannot withstand the high organic solvent concentrations...
Protein-polyelectrolyte complexation: effects of sterically repulsive groups, macromolecular architecture and hierarchical assembly.
Self-assembly of proteins and polyelectrolytes in aqueous solutions is a promising approach for the development of advanced biotherapeutics and engineering efficient biotechnological processes....
Extracting Orientation and Distance-Dependent Interaction Potentials between Proteins in Solutions Using Small-Angle X-ray/Neutron Scattering.
Nonspecific protein-protein interactions (PPIs) are key to understanding the behavior of proteins in solutions. However, experimentally measuring anisotropic PPIs as a function of orientation and...