Videos
NMR approaches for intrinsically disordered proteins
During the 91st session of the Global NMR Discussion Meetings held on November 5th, 2024, via Zoom, Prof. Julie Forman-Kay from the University of Toronto & SickKids Research Institute, Canada, gave a talk on the topic "NMR approaches for intrinsically disordered proteins". The recording serves as a tutorial.
Abstract: NMR is a powerful tool for obtaining site-specific information about dynamic systems, including intrinsically disordered proteins and protein regions (IDPs/IDRs) which do not adopt unique, stable folded structures. While computational approaches are increasingly powerful for stable proteins and protein domains, there is a huge need for experimental information about IDPs, IDRs and the highly dynamic complexes that they often make with other disordered proteins, folded domains and other biomolecules. The lecture will highlight examples of NMR studies of IDPs and their dynamic complexes, including condensed state models of those found in biomolecular condensates.
Find out more about Prof. Julie Forman-Kay's research: https://biochemistry.utoronto.ca/person/julie-d-forman-kay/
Explorations in NMR Relaxation
During the 72nd session of the Global NMR Discussion Meetings held on October 10th, 2023 via Zoom, Prof. Alexej Jerschow gave a talk on the topic "Explorations in NMR Relaxation by Experiments and MD/Ab Initio Computation". The recording serves as a tutorial.
Prof. Alexej Jerschow is a Professor of Chemistry at New York University, USA.
Website: https://wp.nyu.edu/jerschow/
Google scholar: https://scholar.google.com/citations?...
X (previously Twitter): https://twitter.com/ajerschow
Measuring Dynamics Using Anisotropic Interactions in MAS-NMR
During the 68th session of the Global NMR Discussion Meetings held on May 30th, 2023 via Zoom, Dr. Kaustubh Mote gave a talk on the topic "Measuring dynamics using anisotropic interactions in MAS-NMR". The recording serves as a tutorial.
Abstract: Solid-state MAS NMR gives direct access to anisotropic interactions such as CSA, dipole-dipole and quadrupolar couplings. The precise measurement of these interactions, in addition to providing structural features, also gives access to dynamics via their partial averaging due to molecular motion. This tutorial will explore various techniques that are available to extract details of molecular motion via the measurement of these anisotropic interactions, with a particular focus on the measurement of dipole-dipole couplings.
Dr. Kaustubh Mote is a Reader at Tata Institute of Fundamental Research (TIFR) Hyderabad, India.
Website: https://www.tifrh.res.in/~kaustubh/
Google scholar: https://scholar.google.com/citations?...
Twitter: https://twitter.com/kaustubhmote_?lan...
Surprising Consequences of High Electron Spin Polarization
During the 59th session of the Global NMR Discussion Meetings held on January 10th, 2023 via Zoom, Dr. Quentin Chappuis Stern gave a talk on the topic "The surprising consequences of near unity electron spin polarization". The recording serves as a tutorial.
Abstract:
The inherent low sensitivity of NMR can be overcome by hyperpolarization techniques, which increase the polarization of nuclear spins far beyond the Boltzmann equilibrium. One such method is dynamic nuclear polarization (DNP), which consists of transferring the high polarization of unpaired electron spins to surrounding nuclear spins via microwave irradiation. In the case of dissolution DNP (dDNP), the sample is hyperpolarized in the solid state at low temperature (1-2 K) and moderate magnetic field (3-7 T), where the Boltzmann polarization of electron spins approaches unity, translating into equally high nuclear polarization under DNP. In addition to yielding high nuclear polarization, the high electron polarization has other interesting consequences for NMR. Indeed, as the electron polarization tends towards unity, the electron flip-flop probability vanishes, an effect sometimes referred to as “bath quenching”. By switching on and off microwave irradiation (microwave gating), one switches on and off electron flip-flops and hence paramagnetic relaxation. This has been shown to have a dramatic effect on transverse nuclear relaxation and on nuclear spin diffusion. In this talk, I will review the basic concepts of paramagnetic relaxation and its dependence on electron polarization. I will then present experiments where we used microwave gating to perform efficient CP, to detect EPR properties indirectly via NMR properties, and finally to study nuclear spin diffusion in the vicinity of electron spins.
Speaker's biography:
2014- Undergraduate and Masters, EPFL (Switzerland). Thesis with Prof. Bodenhausen
2022- PhD, CRMN Lyon (France), with Prof. Sami Jannin
Follow Dr. Stern's work here:
Twitter: https://twitter.com/quentinchapp
Google scholar: https://scholar.google.fr/citations?u...
Structure & Thermodynamics of Sorption Equilibria using NMR
During the 46th session of the Global NMR Discussion Meetings held on April 5, 2022 via Zoom, Prof. Vincenzo Venditti from Iowa State University gave a talk on the topic "Solution NMR methods for structural and thermodynamic investigation of sorption equilibria". The recording serves as a tutorial.
Abstract:
Nanoparticles are highly tunable materials that owe some of their unique properties to the ability to efficiently and selectively adsorb their target ligands. In this tutorial we will discuss the use of DEST, relaxation dispersion, and R1 experiments for investigating structure, kinetics, and thermodynamics of sorption with atomic resolution.
Venditti group website: https://group.chem.iastate.edu/Venditti/
Google Scholar: https://scholar.google.com/citations?...
Speaker's biography: Vincenzo Venditti received a Ph.D. from the University of Siena in 2009 for his work with Neri Niccolai and Sam Butcher on the surface accessibility of biopolymers. From 2009 to 2014 he was a Postdoctoral Fellow at the National Institutes of Health in the group of Marius Clore where he specialized in biomolecular NMR techniques for the investigation of protein structure, dynamics and interactions. Vincenzo joined the Department of Chemistry at ISU in January 2015.
Methyl Sidechain Probes for Solution NMR of Large Proteins
In session 25 held on 13th April 2021, Dr. Andrew McShan gave a talk on "Utility of Methyl Sidechain Probes for Solution Nuclear Magnetic Resonance (NMR) spectroscopy of large proteins", via Zoom. The video was recorded live during the presentation and serves as an educative lecture.
Follow Dr. McShan's work on Google scholar: https://scholar.google.com/citations?...
Biography: Andrew received a B.S. in Biochemistry and Ph.D. in Molecular, Cellular & Developmental Biology from the University of Kansas with Roberto De Guzman. During their Ph.D., they used methyl-based solution-state NMR to characterize the structure and function of bacterial type III secretion systems. In 2016, they moved to the University of California, Santa Cruz and joined the lab of Nik Sgourakis where methyl NMR was used to elucidate mechanistic aspects of large molecular machines of the adaptive immune system. Currently, Andrew is a postdoctoral fellow at the Children’s Hospital of Philadelphia where they continue to harness the power of methyl NMR to discern the structure and function of proteins complexes of the innate immune system.
Abstract: In recent years, the use of site-specific methyl probes has pushed the molecular weight limit of solution-state NMR to beyond 1 MDa. In this tutorial, we will discuss practical aspects of methyl NMR. The first section will summarize approaches for methyl resonance assignment, including recent advances in automated assignment using methyl-methyl nuclear Overhauser effect measurements. The second section will describe methyl-based NMR methods to uncover biomolecular structure, function and dynamics. Throughout the discussion, a range of large molecular machines where methyl probes have been exploited will be highlighted, including a handful of important immunological protein complexes.
Low-field vs high-field NMR: why not both?
In session 24, held virtually via zoom on 16th March 2021 Dr. Fabien Ferrage gave a talk on the topic "Low-field vs. high-field nuclear magnetic resonance spectroscopy: why not both?". The video was recorded live during the presentation and serves as an educative lecture.
Dr. Ferrage is currently Director of research at CNRS and associate professor at Ecole Normale Supérieure (ENS), Paris, France.
Website: http://www.paris-en-resonance.fr/CvHt...
Twitter: @fabferrage
Google scholar: https://scholar.google.fr/citations?u...
Abstract: High magnetic fields usually provide higher sensitivity and resolution, which are essential to investigate complex systems by NMR. Low-field NMR is cheap, convenient, and sometimes even better than high-field NMR. I will discuss and compare both approaches in the first part of the seminar. In the second part, I will introduce two-field NMR, in which we combine high- and low-field NMR in a single experiment. I will present how two-field NMR works and can lead to better NMR spectra in challenging systems.
Nanoparticle-assisted NMR relaxation in protein dynamics & metabolomics
The 18th session of the Global NMR Discussion Meeting was held on 10th November 2020 via Zoom. Dr. Mouzhe Xie gave a talk on nanoparticle-assisted nuclear magnetic resonance (NMR) relaxation in protein dynamics and metabolomics. The video was recorded live during the presentation and serves as an educative lecture.
Bio: Mouzhe Xie studied chemical biology at Xiamen University (China) from 2009-2013. He received his Ph.D. degree from The Ohio State University (USA) in 2018, where he developed and applied solution NMR spectroscopy to study protein dynamics and metabolomics. He then spent 5 months at EPFL (Switzerland) as a visiting scientist. Currently, he is conducting postdoctoral research on nanoscale NMR and quantum sensing at the University of Chicago (USA).
Personal website: https://sites.google.com/view/xiemouzhe
Google scholar: https://scholar.google.com/citations?...
LinkedIn: https://www.linkedin.com/in/mouzhe-xi...
Abstract: In nanoparticle-assisted solution NMR, synthetic nanoparticles are added to NMR samples, which reduce the reorientational motion of molecules or protein regions in a selective or differential way. This leads to interesting spectral observations that contain critical information about the physicochemical properties, structures, dynamics, and functions of biomolecules. In this tutorial, I will introduce the basics of NMR relaxation theories, followed by some technical details including pulse selection and data processing. The discussion will be buttressed by recent studies on some important topics, such as supra-τc (slow) internal motions of globular proteins, cooperative binding of intrinsically disordered proteins to inorganic surfaces, and accurate metabolite identification in the context of NMR-based metabolomics."
Relaxation-Assisted Spectral Editing in Biological Solid-State NMR
The 10th session of the Global NMR Discussion Meeting was held on 10th July 2020 via Zoom. Dr. Ieva Goldberga gave a talk on the following topic: Relaxation-Assisted Spectral Editing in Solid-State Nuclear Magnetic Resonance (NMR) Spectroscopy of Biological Materials. The video was recorded live during the presentation and serves as an educative lecture.
Dr. Ieva Goldberga is currently a postdoc at the University of Montpellier (France), working in the research group of Dr. Danielle Laurencin. She received her Ph.D. in 2020 from Prof. Melinda Duer's group at the University of Cambridge, U.K.
Follow Dr. Ieva Goldberga on Twitter: @ieva_goldberga
Google Scholar: https://scholar.google.com/citations?...