B-cell lymphoma 2 (Bcl-2) proteins are the main regulators of mitochondrial apoptosis. Anti-apoptotic Bcl-2 proteins possess a hydrophobic tail-anchor enabling them to translocate to their target membrane and to shift into an active conformation where they inhibit pro-apoptotic Bcl-2 proteins to ensure cell survival. To address the unknown molecular basis of their cell-protecting functionality, we used intact human Bcl-2 protein natively residing at the mitochondrial outer membrane and applied...
[NMR paper] Identification and quantification of oxidation products in full-length biotherapeutic antibodies by NMR spectroscopy.
Identification and quantification of oxidation products in full-length biotherapeutic antibodies by NMR spectroscopy.
Related Articles Identification and quantification of oxidation products in full-length biotherapeutic antibodies by NMR spectroscopy.
Anal Chem. 2020 Jun 12;:
Authors: Hinterholzer A, Stanojlovic V, Regl C, Huber CG, Cabrele C, Schubert M
Abstract
Therapeutic proteins are an indispensable class of drugs and often therapeutics of last resort. They are sensitive to oxidation, which is of critical concern, because...
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06-13-2020 05:51 PM
[NMR paper] NMR structure of a full-length single-pass membrane protein NRADD.
NMR structure of a full-length single-pass membrane protein NRADD.
Related Articles NMR structure of a full-length single-pass membrane protein NRADD.
Proteins. 2019 Apr 29;:
Authors: Nadezhdin KD, Goncharuk SA, Arseniev AS, Mineev KS
Abstract
Structural study of any single-pass membrane protein is both an important and challenging task. In this report, we present the structure of a neurotrophin receptor-alike death-domain protein, NRADD. The structure and dynamics of the protein was investigated by conventional nuclear magnetic...
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04-30-2019 03:58 PM
A Novel Domain Assembly Routine for Creating Full-Length Models of Membrane Proteins from Known Domain Structures
A Novel Domain Assembly Routine for Creating Full-Length Models of Membrane Proteins from Known Domain Structures
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00995/20171211/images/medium/bi-2017-00995a_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00995
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/IYVe61xDFY0
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12-12-2017 02:12 AM
[NMR paper] (2)H-NMR and MD Simulations Reveal Membrane-Bound Conformation of Magainin 2 and Its Synergy with PGLa.
(2)H-NMR and MD Simulations Reveal Membrane-Bound Conformation of Magainin 2 and Its Synergy with PGLa.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles (2)H-NMR and MD Simulations Reveal Membrane-Bound Conformation of Magainin 2 and Its Synergy with PGLa.
Biophys J. 2016 Nov 15;111(10):2149-2161
Authors: Strandberg E, Horn D, Reißer S, Zerweck J, Wadhwani P, Ulrich AS
Abstract
Magainin 2 (MAG2) and PGLa are two ?-helical antimicrobial...
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06-13-2017 09:46 PM
[NMR paper] Dynamic Interaction Between Membrane-Bound Full-Length Cytochrome P450 and Cytochrome b5 Observed by Solid-State NMR Spectroscopy.
Dynamic Interaction Between Membrane-Bound Full-Length Cytochrome P450 and Cytochrome b5 Observed by Solid-State NMR Spectroscopy.
Dynamic Interaction Between Membrane-Bound Full-Length Cytochrome P450 and Cytochrome b5 Observed by Solid-State NMR Spectroscopy.
Sci Rep. 2013 Aug 29;3:2538
Authors: Yamamoto K, Dürr UH, Xu J, Im SC, Waskell L, Ramamoorthy A
Abstract
Microsomal monoxygenase enzymes of the cytochrome-P450 family are found in all biological kingdoms, and play a central role in the breakdown of metabolic as well as...
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08-30-2013 04:35 PM
NMR characterization of the C-terminal tail of full-length RAGE in a membrane mimicking environment
NMR characterization of the C-terminal tail of full-length RAGE in a membrane mimicking environment
Abstract Targeting the receptor for the advanced glycation endproducts (RAGE) signalling has a potential for the prevention and treatment of several pathologies. Extracellular activation of RAGE triggers the interactions of the RAGE cytoplasmic tail with intracellular protein partners. Here the cytoplasmic tail of RAGE has been investigated by NMR as part of the full-length protein, in the presence of a membrane-mimicking environment. The isolated cytoplasmic tail has also been studied...
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09-24-2012 01:02 AM
[NMR paper] Functional characterization and NMR spectroscopy on full-length Vpu from HIV-1 prepar
Functional characterization and NMR spectroscopy on full-length Vpu from HIV-1 prepared by total chemical synthesis.
Related Articles Functional characterization and NMR spectroscopy on full-length Vpu from HIV-1 prepared by total chemical synthesis.
J Am Chem Soc. 2004 Mar 3;126(8):2439-46
Authors: Kochendoerfer GG, Jones DH, Lee S, Oblatt-Montal M, Opella SJ, Montal M
Vpu is an 81-residue integral membrane protein encoded in the HIV-1 genome that is of considerable interest because it plays important roles in the release of virus particles...
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11-24-2010 09:25 PM
[NMR paper] NMR assignment of the full-length ribosomal protein L11 from Thermotoga maritima.
NMR assignment of the full-length ribosomal protein L11 from Thermotoga maritima.
Related Articles NMR assignment of the full-length ribosomal protein L11 from Thermotoga maritima.
J Biomol NMR. 2003 Feb;25(2):163-4
Authors: Ilin S, Hoskins A, Schwalbe H, Wöhnert J
Neutron reflectometry and NMR spectroscopy of full-length Bcl-2 protein reveal its membrane localization and conformation
Linear Mode
