Videos
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.
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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.
Chemical biology tools for the NMR structural biologist
Session 23 held virtually via zoom on 2nd March 2021 featured Prof. Galia Debelouchina, Assistant Professor at University of California San Diego (UCSD), U.S.A. Prof. Debelouchina gave a talk on "Chemical biology tools for the Nuclear Magnetic Resonance (NMR) structural biologist ". The video was recorded live during the presentation and serves as an educative lecture.
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Website: http://debelouchinalab.ucsd.edu
Google scholar: https://scholar.google.com/citations?...
Twitter: @GaliaLab
Education 2011 Ph.D., Physical Chemistry, Massachusetts Institute of Technology 2005 B.A., Chemistry, Mathematics, Colby College Appointments 2017 - present Assistant Professor, UCSD 2012 - 2017 Postdoctoral Associate, Chemical Biology, Princeton University
Abstract: Many of the challenging biological problems that NMR spectroscopists study involve large and complex proteins that are also often post-translationally modified. In this tutorial, I will cover NMR friendly approaches to install post-translational modifications efficiently, to segmentally label proteins, and to install various spectroscopic probes in a selective manner. I will cover tools such as inteins and sortase, unnatural amino acid incorporation, native and expressed protein ligation, and bio-orthogonal chemical approaches for protein labeling. I will discuss the advantages and challenges of these tools and present applications from my own lab and the recent literature.
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."
Protein Structure Determination Using Paramagnetic NMR
The 17th session of the Global NMR Discussion Meeting was held on 27th October 2020 via Zoom. Dr. Alireza Bahramzadeh gave a talk on the use of paramagnetic nuclear magnetic resonance (NMR) spectroscopy for protein structure determination. The video was recorded live during the presentation and serves as an educative lecture.
Abstract: The long-range nature of the paramagnetic effects arising from unpaired electrons of metal ions renders them a powerful NMR spectroscopic tool for the study of the structure and dynamics of biological macromolecules. In this tutorial, we will discuss protein structure determination using paramagnetic NMR. The first part will cover different types of paramagnetic metal ions and their paramagnetic effects in NMR, mainly focusing on using techniques which better immobilize metal ions onto the proteins and do not impact the protein structure; the second part will consider Pseudocontact Shifts (PCSs) for determining the 3D structure of proteins.
Biography: Alireza received a bachelor of Chemical Engineering and a master of Polymer engineering from the University of Tehran, Iran. During his master’s project, he worked on developing new nanomembranes for heavy metal ions removal in water. In 2015, he moved to Australia and joined the research group of Professor Gottfried Otting to undertake a Ph.D. During his Ph.D., he worked on developing new ways of studying protein structure using paramagnetic NMR spectroscopy.
Follow Alireza on Twitter: @alireza_bahramz
Google scholar page: https://scholar.google.com/citations?...
Research Gate: https://www.researchgate.net/profile/...