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
CoMD/NMR is founded as a BTRR Center on June 1, 2017.
CoMD/NMR continues as a BTDD Center on July 1, 2022.
Educational materials available: Tutorial on Model-free analysis of 15N relaxation data.
NMR Spectroscopy of Macromolecules taught at NYSBC, Spring 2022.
Ring Dynamics software released.
Rotating Frame Relaxation in Magic Angle Spinning Solid State NMR, a Promising Tool for Characterizing Biopolymer Motion.
Chemical reviews 122 14940-14953 2022 Sep 28
High-Resolution Magic Angle Spinning NMR of KcsA in Liposomes: The Highly Mobile C-Terminus.
Biomolecules 12 2022 Aug 15
Comparisons of Ribonuclease HI Homologs and Mutants Uncover a Multistate Model for Substrate Recognition.
Journal of the American Chemical Society 144 5342-5349 2022 Mar 30
Structural and dynamic studies of the peptidase domain from Clostridium thermocellum PCAT1.
Protein science : a publication of the Protein Society 31 498-512 2022 Feb
Bootstrap Aggregation for Model Selection in the Model-free Formalism.
Magnetic resonance (Gottingen, Germany) 2 251-264 2021
Approximate Representations of Shaped Pulses Using the Homotopy Analysis Method.
Magnetic resonance (Gottingen, Germany) 2 175-186 2021
Dynamics in natural and designed elastins and their relation to elastic fiber structure and recoil.
Biophysical journal 120 4623-4634 2021 Oct 19