[NMR paper] The advanced properties of circularized MSP nanodiscs facilitate high-resolution NMR studies of membrane proteins
The advanced properties of circularized MSP nanodiscs facilitate high-resolution NMR studies of membrane proteins
Membrane mimetics are essential for structural and functional studies of membrane proteins. A promising lipid-based system are phospholipid nanodiscs, where two copies of a so-called membrane scaffold protein (MSP) wrap around a patch of lipid bilayer. Consequently, the size of a nanodisc is determined by the length of the MSP. Furthermore, covalent MSP circularization was reported to improve nanodisc stability. However, a more detailed comparative analysis of the biophysical...
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10-26-2022 07:20 AM
[NMR paper] Lipid Nanodiscs for High-Resolution NMR Studies of Membrane Proteins
Lipid Nanodiscs for High-Resolution NMR Studies of Membrane Proteins
Membrane proteins (MPs) play essential roles in numerous cellular processes. Because around 70% of the currently marketed drugs target MPs, a detailed understanding of their structure, binding properties, and functional dynamics in a physiologically relevant environment is crucial for a more detailed understanding of this important protein class. We here summarize the benefits of using lipid nanodiscs for NMR structural investigations and provide a detailed overview of the currently used lipid...
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10-20-2021 06:28 AM
[ASAP] High-Resolution In Situ NMR Spectroscopy of Bacterial Envelope Proteins in Outer Membrane Vesicles
High-Resolution In Situ NMR Spectroscopy of Bacterial Envelope Proteins in Outer Membrane Vesicles
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.9b01123/20200406/images/medium/bi9b01123_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.9b01123
http://feeds.feedburner.com/~r/acs/bichaw/~4/2_SiKyocUYc
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04-07-2020 07:35 PM
[NMR paper] High-resolution in-situ NMR spectroscopy of bacterial envelope proteins in outer membrane vesicles.
High-resolution in-situ NMR spectroscopy of bacterial envelope proteins in outer membrane vesicles.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles High-resolution in-situ NMR spectroscopy of bacterial envelope proteins in outer membrane vesicles.
Biochemistry. 2020 Apr 01;:
Authors: Thoma J, Burmann BM
Abstract
The cell envelope of Gram-negative bacteria is an elaborate cellular environment, consisting of two lipid membranes separated by the aqueous...
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04-03-2020 09:41 PM
Super resolution NOESY spectra of proteins
Super resolution NOESY spectra of proteins
Abstract
Spectral resolution remains one of the most significant limitations in the NMR study of biomolecules. We present the srNOESY (super resolution nuclear overhauser effect spectroscopy) experiment, which enhances the resolution of NOESY cross-peaks at the expense of the diagonal peak line-width. We studied two proteins, ubiquitin and the influenza hemagglutinin fusion peptide in bicelles, and we achieved average resolution enhancements of 21â??47% and individual peak enhancements as large as ca. 450%....
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04-30-2019 03:58 PM
[NMR paper] High-Resolution NMR Determination of the Dynamic Structure of Membrane Proteins.
High-Resolution NMR Determination of the Dynamic Structure of Membrane Proteins.
High-Resolution NMR Determination of the Dynamic Structure of Membrane Proteins.
Angew Chem Int Ed Engl. 2016 Jul 27;
Authors: Jaremko M, Jaremko ?, Villinger S, Schmidt CD, Griesinger C, Becker S, Zweckstetter M
Abstract
(15) N spin-relaxation rates are demonstrated to provide critical information about the long-range structure and internal motions of membrane proteins. Combined with an improved calculation method, the relaxation-rate-derived...
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07-28-2016 12:07 PM
Topologically Diverse Human Membrane Proteins Partitionto Liquid-Disordered Domains in Phase-Separated Lipid Vesicles
Topologically Diverse Human Membrane Proteins Partitionto Liquid-Disordered Domains in Phase-Separated Lipid Vesicles
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01154/20160210/images/medium/bi-2015-01154x_0003.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01154
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/FqvhNKDI0Xk
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02-11-2016 10:30 PM
[NMR paper] High-resolution NMR spectroscopy of membrane proteins in aligned bicelles.
High-resolution NMR spectroscopy of membrane proteins in aligned bicelles.
Related Articles High-resolution NMR spectroscopy of membrane proteins in aligned bicelles.
J Am Chem Soc. 2004 Dec 1;126(47):15340-1
Authors: De Angelis AA, Nevzorov AA, Park SH, Howell SC, Mrse AA, Opella SJ
High-resolution solid-state NMR spectra can be obtained from uniformly (15)N-labeled membrane proteins in magnetically aligned bicelles. Fast uniaxial diffusion about the axis of the bilayer normal results in single-line spectra that contain the orientational...