The Center on Macromolecular Dynamics by NMR Spectroscopy (CoMD/NMR) is a Biomedical Technology Development and Dissemination (BTDD) Center supported by U.S. National Institutes of Health grant 1RM1 GM145397 and located at the New York Structural Biology Center (NYSBC). The mission of CoMD/NMR is to develop methods for studying how the conformations and dynamics of proteins, nucleic acids mediate their biological functions, when bound to drugs or toxins, or when diseases occur. CoMD/NMR uses NMR spectrometers, machines very similar to MRI machines used by physicians to provide pictures of the human body. NYSBC has nine NMR spectrometers of different sizes and is one of the largest such centers in the world. Scientists at CoMD/NMR research and implement new methods for performing such studies and assist scientists from around the U.S. in using NMR spectroscopy in their own research. Technology developed at CoMD/NMR has been used to study amyloid diseases, behavior of protein ion channels in the nervous system, formation of distinct tissues during development of the mammalian body, function and regulation of proteins involved in metabolism, and other biological processes.
Staff Technology Collaboration Education Dissemination GalleryCoMD/NMR is founded as a BTRR Center on June 1, 2017.
CoMD/NMR continues as a BTDD Center on July 1, 2022.
NMR Spectroscopy of Macromolecules taught at NYSBC, Spring 2024.
Ring Dynamics software V1.19 released 02/02/2024
Visit CoMD/NMR at ENC (Willow Living Room, First Floor)
NMRFx: Integrated Software for NMR Data Processing, Visualization, Analysis and Structure Calculation.
bioRxiv : the preprint server for biology 2025 Aug 29
An A-T Hoogsteen Base Pair in a Naked DNA Hairpin Motif: A Protein-Recognized Conformation.
Angewandte Chemie (International ed. in English) 64 e202425067 2025 Jun 17
Spatially resolved DNP-assisted NMR illuminates the conformational ensemble of α-synuclein in intact viable cells.
Proceedings of the National Academy of Sciences of the United States of America 122 e2500367122 2025 Jun 10
Binding of small molecules at the P-stalk site of ricin A subunit trigger conformational changes that extend into the active site.
The Journal of biological chemistry 301 108310 2025 Mar
Allosteric regulation of the tyrosine phosphatase PTP1B by a protein-protein interaction.
Protein science : a publication of the Protein Society 34 e70016 2025 Jan
Deuterium spin relaxation of fractionally deuterated ribonuclease H using paired 475 and 950 MHz NMR spectrometers.
Journal of biomolecular NMR 78 169-177 2024 Sep
Resolution in cryogenic solid state NMR: Challenges and solutions.
Protein science : a publication of the Protein Society 33 e4803 2024 Jul
(1)H, (13)C, and (15)N backbone and methyl group resonance assignments of ricin toxin A subunit.
Biomolecular NMR assignments 18 85-91 2024 Jun
Quantitative and systematic NMR measurements of sequence-dependent A-T Hoogsteen dynamics uncovers unique conformational specificity in the DNA double helix.
bioRxiv : the preprint server for biology 2024 May 15
Direct Measurement of 8OG Syn-Anti Flips in Mutagenic 8OG·A and Long-Range Damage-Dependent Hoogsteen Breathing Dynamics Using (1)H CEST NMR.
The journal of physical chemistry. B 128 4087-4096 2024 May 2