Dr. John Schiel holding a figure of the NISTmAb
Excellence in Research...
IBBR scientists lead ground-breaking research, technology development and standards programs that advance and support the fields of biotechnology, biomanufacturing and human health.
A state-of-the-art SAXSLAB’s GANESHA on display here at IBBR
State-of-the-Art Methods...
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.
Dr. Brian Pierce analyzing data with a figure of prostate-specific membrane antigen (PSMA) on his desk
Fostering Collaboration...
IBBR supports a dynamic research environment that facilitates interactions and collaborations between our scientists, partners, and stakeholders; promoting new research directions that complement and build on existing strengths.

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...

AD-X2 Controversy Screening at IBBR - November 20th

On Wednesday, November 20th at 3:00pm, IBBR will host a screening of the documentary "The AD-X2 Controversy." Set in the 1950s, during a time of booming economy and rapid scientific advancement, this 23-minute film tells the captivating story of a charismatic salesman who sought to profit from a chemical additive...

Eunkyoung Kim in Payne Lab Awarded Best Paper by the Advances in Redox Research Journal

Dr. Eunkyoung Kim, Research Assistant Professor in the Payne Lab at University of Maryland College Park and IBBR, was awarded the Best Paper of the Year by the Advances in Redox Research journal. This peer-reviewed interdisciplinary journal published close to thirty papers in 2023 with a range of studies of...

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.

Read More

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.

Read More

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.

Read More

Various models of molecules
309
Current Members
171
Post-Docs Mentored
1435
Publications

Upcoming Events

NIST Group Meeting; Kinjal Mondal

Monday, November 25, 2024 - 11:00am

BMD Staff Seminar L. Borsuk/ I. Karageorgos, .06/.07

L. Borsuk/ I. Karageorgos, .06/.07

Tuesday, December 3, 2024 - 11:00am

NIST Group Meeting; Ibhan Sharma

Wednesday, December 4, 2024 - 11:00am

Recent Publications

Toripalimab Plus Chemotherapy as a First-Line Therapy for Extensive-Stage Small Cell Lung Cancer: The Phase 3 EXTENTORCH Randomized Clinical Trial.

IMPORTANCE

Patients with extensive-stage small cell lung cancer (ES-SCLC) have poor prognoses and unmet medical needs.

OBJECTIVE

To evaluate the efficacy and safety of toripalimab plus etoposide...

Revised 4-Point Water Model for the Classical Drude Oscillator Polarizable Force Field: SWM4-HLJ.

In this work the 4-point polarizable SWM4 Drude water model is reparametrized. Multiple models were developed using different strategies toward reproduction of specific target data. Results...

Biomimetic Redox Capacitor To Control the Flow of Electrons.

In biological systems, electrons, energy, and information "flow" through the redox modality, and we ask, does biology have redox capacitor capabilities for storing electrons? We describe emerging...

modXNA: A Modular Approach to Parametrization of Modified Nucleic Acids for Use with Amber Force Fields.

Modified nucleic acids have surged as a popular therapeutic route, emphasizing the importance of nucleic acid research in drug discovery and development. Beyond well-known RNA vaccines, antisense...

A fitness distribution law for amino-acid replacements.

The effect of replacing the amino acid at a given site in a protein is difficult to predict. Yet, evolutionary comparisons have revealed highly regular patterns of interchangeability between pairs...