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A RedAlgal Bourbonane Sesquiterpene Synthase Definedby Microgram-Scale NMR-Coupled Crystalline Sponge X-ray DiffractionAnalysis
Nov 15, 2017 - 8:36 AM - by nmrlearner
nmrlearner's Avatar A RedAlgal Bourbonane Sesquiterpene Synthase Definedby Microgram-Scale NMR-Coupled Crystalline Sponge X-ray DiffractionAnalysis

Roland D. Kersten, Shoukou Lee, Daishi Fujita, Toma?s? Pluskal, Susan Kram, Jennifer E. Smith, Takahiro Iwai, Joseph P. Noel, Makoto Fujita and Jing-Ke Weng



Journal of the American Chemical Society
DOI: 10.1021/jacs.7b09452




Source: Journal of the American Chemical Society
0 Replies | 15 Views
Probing the cooperativity of Thermoplasma acidophilum proteasome core particle gating by NMR spectroscopy [Biophysics and Computational Biology]
Nov 15, 2017 - 8:36 AM - by nmrlearner
nmrlearner's Avatar Probing the cooperativity of Thermoplasma acidophilum proteasome core particle gating by NMR spectroscopy [Biophysics and Computational Biology]

Rui Huang, Felipe Perez, Lewis E. Kay...
Date: 2017-11-14

The 20S proteasome core particle (20S CP) plays an integral role in cellular homeostasis by degrading proteins no longer required for function. The process is, in part, controlled via gating residues localized to the ends of the heptameric barrel-like CP structure that occlude substrate entry pores, preventing unregulated degradation of... Read More


PNAS:
Number: 46
Volume: 114
0 Replies | 17 Views
Binding kinetics and substrate selectivity in HIV-1 protease-Gag interactions probed at atomic resolution by chemical exchange NMR [Biophysics and Computational Biology]
Nov 15, 2017 - 8:36 AM - by nmrlearner
nmrlearner's Avatar Binding kinetics and substrate selectivity in HIV-1 protease-Gag interactions probed at atomic resolution by chemical exchange NMR [Biophysics and Computational Biology]

Lalit Deshmukh, Vitali Tugarinov, John M. Louis, G. Marius Clore...
Date: 2017-11-14

The conversion of immature noninfectious HIV-1 particles to infectious virions is dependent upon the sequential cleavage of the precursor group-specific antigen (Gag) polyprotein by HIV-1 protease. The precise mechanism whereby protease recognizes distinct Gag cleavage sites, located in the intrinsically disordered linkers connecting the globular domains of Gag, remains unclear.... Read More


PNAS:
Number: 46
Volume: 114
0 Replies | 21 Views
Pick up a prion: Solid state NMR spots the differences
Nov 15, 2017 - 8:36 AM - by nmrlearner
nmrlearner's Avatar Pick up a prion: Solid state NMR spots the differences

Researchers in the USA have used solid-state nuclear magnetic resonance (NMR) spectroscopy to study the rogue proteins involved in familial human cerebral amyloid angiopathy (CAA). This hereditary neurodegenerative condition is one of the family of prion diseases that afflict mammals and include bovine spongiform encephalopathy (often referred to colloquially as "mad cow disease"), Creutzfeldt-Jakob disease in humans, their equivalents in cats, mice, hamsters and other animals.

Read the rest at Spectroscopynow.com
0 Replies | 35 Views
Biological Roles of Protein Kinetic Stability
Nov 14, 2017 - 4:20 PM - by nmrlearner
nmrlearner's Avatar Biological Roles of Protein Kinetic Stability



Biochemistry
DOI: 10.1021/acs.biochem.7b00942



More...
0 Replies | 128 Views
[NMR paper] Formation of the chaperonin complex studied by 2D NMR spectroscopy.
Nov 14, 2017 - 4:20 PM - by nmrlearner
nmrlearner's Avatar Formation of the chaperonin complex studied by 2D NMR spectroscopy.

Related Articles Formation of the chaperonin complex studied by 2D NMR spectroscopy.

PLoS One. 2017;12(10):e0187022

Authors: Takenaka T, Nakamura T, Yanaka S, Yagi-Utsumi M, Chandak MS, Takahashi K, Paul S, Makabe K, Arai M, Kato K, Kuwajima K

Abstract
We studied the interaction between GroES and a single-ring mutant (SR1) of GroEL by the NMR titration of 15N-labeled GroES with SR1 at three different temperatures (20, 25 and 30°C) in the presence of 3 mM ADP in 100 mM KCl and 10 mM MgCl2 at pH 7.5. We used SR1 instead of wild-type double-ring GroEL to precisely control the stoichiometry of the GroES binding to be... [Read More]
0 Replies | 21 Views
[NMR paper] A De Novo Heterodimeric Due Ferri Protein Minimizes the Release of Reactive Intermediates in Dioxygen-Dependent Oxidation
Nov 14, 2017 - 4:20 PM - by nmrlearner
nmrlearner's Avatar A De Novo Heterodimeric Due Ferri Protein Minimizes the Release of Reactive Intermediates in Dioxygen-Dependent Oxidation


Metalloproteins utilize O2 as an oxidant, and they often achieve a 4-electron reduction without H2O2 or oxygen radical release. Several proteins have been designed to catalyze one or two-electron oxidative chemistry, but the de novo design of a protein that catalyzes the net 4-electron reduction of O2 has not been reported yet. We report the construction of a diiron-binding four-helix bundle, made up of two different covalently linked ?2 monomers, through click chemistry. Surprisingly, the prototype protein, DF-C1, showed a large divergence in its reactivity from earlier DFs (DF: due ferri, two iron). DFs release the quinone imine and free H2O2 in the oxidation of 4-aminophenol in the presence of O2, whereas FeIII-DF-C1 sequesters the quinone imine into the active site, and catalyzes inside the scaffold an oxidative coupling between oxidized and reduced 4-aminophenol. The asymmetry of the scaffold allowed a fine-engineering of the substrate binding pocket, that ensures selectivity.Not just a four-helix bundle: The use of a diiron-binding four-helix bundle scaffold with an asymmetric active site leads to an enhancement in selectivity of the iron-catalyzed oxidative coupling of phenols. The stabilization of the oxidized intermediate in the binding pocket enables the net four-electron O2 reduction, without release of any detectable H2O2.

More...
0 Replies | 21 Views
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