Center on Macromolecular Dynamics by NMR Spectroscopy

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 Gallery

News and Events

CoMD/NMR History

CoMD/NMR is founded as a BTRR Center on June 1, 2017.
CoMD/NMR continues as a BTDD Center on July 1, 2022.

Education

Educational materials available: Tutorial on Model-free analysis of 15N relaxation data.

Education

NMR Spectroscopy of Macromolecules taught at NYSBC, Spring 2022.

Software

Ring Dynamics software released.

Recent Publications

Comparisons of Ribonuclease HI Homologs and Mutants Uncover a Multistate Model for Substrate Recognition.
Martin JA, Palmer AG 3rd Journal of the American Chemical Society 144 5342-5349 2022 Mar 30

Structural and dynamic studies of the peptidase domain from Clostridium thermocellum PCAT1.
Bhattacharya S, Palillo A Protein science : a publication of the Protein Society 31 498-512 2022 Feb

Bootstrap Aggregation for Model Selection in the Model-free Formalism.
Crawley T, Palmer AG 3rd Magnetic resonance (Gottingen, Germany) 2 251-264 2021

Approximate Representations of Shaped Pulses Using the Homotopy Analysis Method.
Crawley T, Palmer AG 3rd Magnetic resonance (Gottingen, Germany) 2 175-186 2021

Dynamics in natural and designed elastins and their relation to elastic fiber structure and recoil.
Carvajal MFCA, Preston JM, Jamhawi NM, Sabo TM, Bhattacharya S, Aramini JM, Wittebort RJ, Koder RL Biophysical journal 120 4623-4634 2021 Oct 19

All CoMD/NMR publications at PubMed