Structural Basis for the Serratia marcescens Lipase Secretion System: Crystal Structures of the Membrane FusionProtein and Nucleotide-Binding Domain
Structural Basis for the Serratia marcescens Lipase Secretion System: Crystal Structures of the Membrane FusionProtein and Nucleotide-Binding Domain
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00985/20171109/images/medium/bi-2017-00985x_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00985
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nmrlearner
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11-11-2017 07:52 AM
[NMR paper] Highly Ordered Self-Assembly of Native Proteins into 1D, 2D, and 3D Structures Modulated by the Tether Length of Assembly-Inducing Ligands
Highly Ordered Self-Assembly of Native Proteins into 1D, 2D, and 3D Structures Modulated by the Tether Length of Assembly-Inducing Ligands
In nature, proteins are organized into highly ordered self-assembled structures with various morphologies and dimensions. In their Communication (DOI: 10.1002/anie.201703052), Y. Ma, G. Chen, and co-workers report the fabrication of protein assemblies by using native protein LecA as a building block through sugar–protein interactions and rhodamine dimerization. The morphologies and dimensions of the protein assemblies can be controlled by the length...
nmrlearner
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07-19-2017 01:32 PM
Solution Behavior of the Intrinsically DisorderedN-Terminal Domain of Retinoid X Receptor ? in the Contextof the Full-Length Protein
Solution Behavior of the Intrinsically DisorderedN-Terminal Domain of Retinoid X Receptor ? in the Contextof the Full-Length Protein
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01122/20160315/images/medium/bi-2015-011224_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01122
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nmrlearner
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03-16-2016 02:51 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...
nmrlearner
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09-24-2012 01:02 AM
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
J Struct Funct Genomics. 2011 Sep 9;
Authors: Yang Y, Ramelot TA, Cort JR, Wang H, Ciccosanti C, Jiang M, Janjua H, Acton TB, Xiao R, Everett JK, Montelione GT, Kennedy MA
Abstract
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nmrlearner
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09-10-2011 06:51 PM
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
J Struct Funct Genomics. 2010 Dec 14;
Authors: Mani R, Vorobiev S, Swapna GV, Neely H, Janjua H, Ciccosanti C, Xiao R, Acton TB, Everett JK, Hunt J, Montelione GT
The conserved Lipoprotein-17 domain of membrane-associated protein Q9PRA0_UREPA from Ureaplasma parvum was selected for structure determination by the Northeast Structural...
nmrlearner
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12-15-2010 12:03 PM
The ?-helical C-terminal domain of full-length recombinant PrP converts to an in-regi
The ?-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel ?-sheet structure in PrP fibrils: Evidence from solid state NMR.
Related Articles The ?-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel ?-sheet structure in PrP fibrils: Evidence from solid state NMR.
Biochemistry. 2010 Oct 6;
Authors: Tycko R, Savtchenko R, Ostapchenko VG, Makarava N, Baskakov IV
We report the results of solid state nuclear magnetic (NMR) measurements on amyloid fibrils formed by the...
A Novel Domain Assembly Routine for Creating Full-Length Models of Membrane Proteins from Known Domain Structures
Linear Mode
