Nanodiscs versus Macrodiscs for NMR of Membrane Proteins
Nanodiscs versus Macrodiscs for NMR of Membrane Proteins
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Biochemistry
DOI: 10.1021/bi201289c
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nmrlearner
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09-30-2011 08:01 PM
Nanodiscs vs. Macrodiscs for NMR of Membrane Proteins.
Nanodiscs vs. Macrodiscs for NMR of Membrane Proteins.
Nanodiscs vs. Macrodiscs for NMR of Membrane Proteins.
Biochemistry. 2011 Sep 21;
Authors: Park SH, Berkamp S, Cook GA, Chan MK, Viadiu H, Opella SJ
Abstract
It is challenging to find membrane mimics that stabilize the native structure, dynamics, and functions of membrane proteins. In a recent advance, nanodiscs have been shown to provide a bilayer environment compatible with solution NMR. Increasing the lipid to "belt" peptide ratio expands their diameter, slows their reorientation...
nmrlearner
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09-23-2011 05:30 PM
[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...
nmrlearner
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11-24-2010 09:25 PM
[NMR paper] Preparation, characterization, and NMR spectroscopy of encapsulated proteins dissolve
Preparation, characterization, and NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids.
Related Articles Preparation, characterization, and NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids.
J Biomol NMR. 2003 Apr;25(4):313-23
Authors: Babu CR, Flynn PF, Wand AJ
Encapsulating a protein in a reverse micelle and dissolving it in a low-viscosity solvent can lower the rotational correlation time of a protein and thereby provides a novel strategy for studying proteins in a variety of contexts. The...
nmrlearner
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11-24-2010 09:01 PM
[NMR paper] An NMR investigation of solution aggregation reactions preceding the misassembly of a
An NMR investigation of solution aggregation reactions preceding the misassembly of acid-denatured cold shock protein A into fibrils.
Related Articles An NMR investigation of solution aggregation reactions preceding the misassembly of acid-denatured cold shock protein A into fibrils.
J Mol Biol. 1999 Sep 3;291(5):1191-206
Authors: Alexandrescu AT, Rathgeb-Szabo K
At pH 2.0, acid-denatured CspA undergoes a slow self-assembly process, which results in the formation of insoluble fibrils. 1H-15N HSQC, 3D HSQC-NOESY, and 15N T2 NMR experiments have...
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11-18-2010 08:31 PM
NMR-Spectroscopic and Solid-State Investigations of Cometal-Free Asymmetric Conjugate
NMR-Spectroscopic and Solid-State Investigations of Cometal-Free Asymmetric Conjugate Addition: A Dinuclear Paracyclophaneimine Zinc Methyl Complex
S. Ay et al
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1032502/aop/images/medium/ja-2010-032502_0003.gifJournal of the American Chemical Society, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable).
Source: Journal of the American Chemical Society
nmrlearner
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09-01-2010 10:56 AM
[NMR paper] NMR investigation of the solution conformation of oxidized flavodoxin from Desulfovib
NMR investigation of the solution conformation of oxidized flavodoxin from Desulfovibrio vulgaris. Determination of the tertiary structure and detection of protein-bound water molecules.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR investigation of the solution conformation of oxidized flavodoxin from Desulfovibrio vulgaris. Determination of the tertiary structure and detection of protein-bound water molecules.
Eur J Biochem. 1996 Jun...
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08-22-2010 02:27 PM
Assessment of GABARAP self-association by its diffusion properties
Abstract Gamma-aminobutyric acid type A receptor-associated protein (GABARAP) belongs to a family of small ubiquitin-like adaptor proteins implicated in intracellular vesicle trafficking and autophagy. We have used diffusion-ordered nuclear magnetic resonance spectroscopy to study the temperature and concentration dependence of the diffusion properties of GABARAP. Our data suggest the presence of distinct conformational states and provide support for self-association of GABARAP molecules. Assuming a monomerâ??dimer equilibrium, a temperature-dependent dissociation constant could be derived....
Preparation of a functional GABARAP-lipid conjugate in nanodiscs and its investigation by solution NMR spectroscopy.
Linear Mode
