A unique ?-expanded reaction cavity tethering a polycyclic moiety which provides a platform for substrate binding was constructed within the robust ?-barrel structure of nitrobindin (NB). NB variants with the cavities of different sizes and shapes are coupled with N-(1-pyrenyl)maleimide (Pyr) to prepare a series of NB-Pyr conjugates. The orientation of the pyrene moiety is fixed within the cavity by the coupling reaction. The fluorescent quenching analysis of NB-Pyr indicates that azachalcone (aza), which is a dienophile for a Diels-Alder (DA) reaction, is efficiently incorporated within the pyrene-linked reaction cavity by the aromatic interaction. The DA reaction between aza and cyclopentadiene proceeds within the reaction cavity of NB-Pyr in the presence Cu(II) ion in high yield and high enantio- and regioselectivity.
A Gradient of Sitewise Diversity Promotes EvolutionaryFitness for Binder Discovery in a Three-Helix Bundle Protein Scaffold
A Gradient of Sitewise Diversity Promotes EvolutionaryFitness for Binder Discovery in a Three-Helix Bundle Protein Scaffold
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b01142/20170309/images/medium/bi-2016-01142g_0015.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b01142
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03-10-2017 03:24 AM
[NMR paper] Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR.
Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR.
Related Articles Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR.
J Biomol NMR. 2015 Jan 30;
Authors: Eddy MT, Su Y, Silvers R, Andreas L, Clark L, Wagner G, Pintacuda G, Emsley L, Griffin RG
Abstract
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01-31-2015 04:16 PM
Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR
Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR
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The human voltage dependent anion channel 1 (VDAC) is a 32Â*kDa β-barrel integral membrane protein that controls the transport of ions across the outer mitochondrial membrane. Despite the determination of VDAC solution and diffraction structures, a structural basis for the mechanism of its function is not yet fully understood. Biophysical studies suggest VDAC requires a lipid bilayer to achieve full function, motivating the need...
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01-30-2015 12:15 PM
[NMR paper] Cavity as a Source of Conformational Fluctuation and High-Energy State: High-Pressure NMR Study of a Cavity-Enlarged Mutant of T4Lysozyme.
Cavity as a Source of Conformational Fluctuation and High-Energy State: High-Pressure NMR Study of a Cavity-Enlarged Mutant of T4Lysozyme.
Cavity as a Source of Conformational Fluctuation and High-Energy State: High-Pressure NMR Study of a Cavity-Enlarged Mutant of T4Lysozyme.
Biophys J. 2015 Jan 6;108(1):133-145
Authors: Maeno A, Sindhikara D, Hirata F, Otten R, Dahlquist FW, Yokoyama S, Akasaka K, Mulder FA, Kitahara R
Abstract
Although the structure, function, conformational dynamics, and controlled thermodynamics of proteins...
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Diels-Alder reactionâ??triggered bioorthogonal protein decaging in living cells - Nature.com
Diels-Alder reactionâ??triggered bioorthogonal protein decaging in living cells - Nature.com
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Diels-Alder reactionâ??triggered bioorthogonal protein decaging in living cells
Nature.com
A generally applicable strategy, however, remains elusive. Herein we describe a small moleculeâ??triggered bioorthogonal protein decaging technique that relies on the inverse electron-demand Diels-Alder reaction for eliminating a chemically caged protein ...
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[NMR paper] Clusters of Branched Aliphatic Side Chains Serve As Cores of Stability in the Native State of the HisF TIM Barrel Protein.
Clusters of Branched Aliphatic Side Chains Serve As Cores of Stability in the Native State of the HisF TIM Barrel Protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Clusters of Branched Aliphatic Side Chains Serve As Cores of Stability in the Native State of the HisF TIM Barrel Protein.
J Mol Biol. 2013 Jan 16;
Authors: Gangadhara BN, Laine JM, Kathuria SV, Massi F, Matthews CR
Abstract
Imidazole-3-glycerol phosphate synthase is a heterodimeric allosteric...
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[NMR paper] Probing the hydrophobic cavity of lipid transfer protein from Nicotiana tabacum throu
Probing the hydrophobic cavity of lipid transfer protein from Nicotiana tabacum through xenon-based NMR spectroscopy.
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J Am Chem Soc. 2004 Dec 8;126(48):15738-46
Authors: Dubois L, Da Silva P, Landon C, Huber JG, Ponchet M, Vovelle F, Berthault P, Desvaux H
The hydrophobic cavity of Lipid Transfer Protein 1 from Nicotiana tabacum is investigated in detail by NMR using xenon as a spy. The analysis of the (129)Xe...
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[NMR paper] Demonstration of positionally disordered water within a protein hydrophobic cavity by
Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR.
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Science. 1995 Mar 24;267(5205):1813-7
Authors: Ernst JA, Clubb RT, Zhou HX, Gronenborn AM, Clore GM
The presence and location of water of hydration (that is, bound water) in the solution structure of human interleukin-1 beta (hIL-1 beta) was investigated with water-selective two-dimensional heteronuclear magnetic resonance spectroscopy. It is shown...
A Pyrene-linked Cavity within a ?-Barrel Protein Promotes an Asymmetric Diels-Alder Reaction
Linear Mode
