Hepatitis D virus (HDV) is a defective virus that relies on hepatitis B virus envelope proteins to complete its replication cycle. The HDV genome contains two isoforms of hepatitis delta antigen: the small and the large hepatitis delta antigens (S- and L-HDAg). Here we report the ¹H, ^(13)C and ^(15) N backbone and side chain resonance assignments of an N-terminally truncated form of S-HDAg (S^(?60)), which lacks the 1-60 oligomerization domain. We derived secondary structures based on NMR...
[NMR paper] 1H, 13C, 15*N backbone and side-chain NMR assignments for three MAX effectors from Magnaporthe oryzae
1H, 13C, 15*N backbone and side-chain NMR assignments for three MAX effectors from Magnaporthe oryzae
Effectors are small and very diverse proteins secreted by fungi and translocated in plant cells during infection. Among them, MAX effectors (for Magnaporthe Avrs and ToxB) were identified as a family of effectors that share an identical fold topology despite having highly divergent sequences. They are mostly secreted by ascomycetes from the Magnaporthe genus, a fungus that causes the rice blast, a plant disease leading to huge crop losses. As rice is the first source of calories in many......
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[NMR paper] Unambiguous Side-Chain Assignments for Solid-State NMR Structure Elucidation of Nondeuterated Proteins via a Combined 5D/4D Side-Chain-to-Backbone Experiment
Unambiguous Side-Chain Assignments for Solid-State NMR Structure Elucidation of Nondeuterated Proteins via a Combined 5D/4D Side-Chain-to-Backbone Experiment
Owing to fast-magic-angle-spinning technology, proton-detected solid-state NMR has been facilitating the analysis of insoluble, crystalline, sedimented, and membrane proteins. However, potential applications have been largely restricted by limited access to side-chain resonances. The recent availability of spinning frequencies exceeding 100 kHz in principle now allows direct probing of all protons without the need for partial...
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[NMR paper] Backbone and side-chain (1)H, (13)C, and (15)N NMR assignments of the N-terminal domain of Escherichia coli LpoA.
Backbone and side-chain (1)H, (13)C, and (15)N NMR assignments of the N-terminal domain of Escherichia coli LpoA.
Related Articles Backbone and side-chain (1)H, (13)C, and (15)N NMR assignments of the N-terminal domain of Escherichia coli LpoA.
Biomol NMR Assign. 2014 Feb 4;
Authors: Jean NL, Bougault C, Derouaux A, Callens G, Vollmer W, Simorre JP
Abstract
The peptidoglycan is a major component of the bacterial cell wall and is essential to maintain cellular integrity and cell shape. Penicillin-Binding Proteins (PBPs) catalyze the final...
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02-05-2014 06:08 PM
[NMR paper] Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28.
Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28.
Related Articles Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28.
Biomol NMR Assign. 2013 Dec 24;
Authors: Peterson TA, Yu L, Piper RC
Abstract
Vps28 is one of four cytosolic proteins comprising the endosomal sorting complex required for transport I (ESCRT-I). ESCRT-I is involved in sorting ubiquitinated proteins to multivesicular bodies as well as in mediating budding of retroviruses. Here, we report the backbone...
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12-25-2013 03:39 PM
[NMR paper] (1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of BPSL1050 from Burkholderia pseudomallei.
(1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of BPSL1050 from Burkholderia pseudomallei.
Related Articles (1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of BPSL1050 from Burkholderia pseudomallei.
Biomol NMR Assign. 2013 Apr 25;
Authors: Gaudesi D, Quilici G, Musco G
Abstract
BPSL1050 is a 13.9*kDa protein produced by the Gram-negative bacterium Burkholderia pseudomallei, the etiological agent of melioidosis. Immunodetection assays against sera patients using protein microarray suggest BPSL1050...
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04-26-2013 12:10 PM
[NMR paper] Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic t
Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic transmembrane light-harvesting 2 protein complex by solid-state Magic Angle Spinning NMR spectroscopy.
Related Articles Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic transmembrane light-harvesting 2 protein complex by solid-state Magic Angle Spinning NMR spectroscopy.
J Biomol NMR. 2005 Apr;31(4):279-93
Authors: Gammeren AJ, Hulsbergen FB, Hollander JG, Groot HJ
This study reports the sequence specific chemical shifts...
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[NMR paper] Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts
Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c.
Related Articles Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c.
Protein Sci. 2003 Sep;12(9):2104-8
Authors: Liu W, Rumbley J, Englander SW, Wand AJ
The mutant of horse heart cytochrome c was expressed in E. coli during growth on isotopically enriched minimal media. Complete resonance assignments of both the diamagnetic reduced (spin zero) and paramagnetic oxidized (spin (1/2))...
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[NMR paper] Backbone and side-chain 13C and 15N signal assignments of the alpha-spectrin SH3 doma
Backbone and side-chain 13C and 15N signal assignments of the alpha-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 Tesla.
Related Articles Backbone and side-chain 13C and 15N signal assignments of the alpha-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 Tesla.
Chembiochem. 2001 Apr 2;2(4):272-81
Authors: Pauli J, Baldus M, van Rossum B, de Groot H, Oschkinat H
The backbone and side-chain 13C and 15N signals of a solid 62-residue (u-13C,15N)-labelled protein containing the alpha-spectrin SH3 domain were...
1H, 15N and 13C backbone and side chain solution NMR assignments of the truncated small hepatitis delta antigen ?60-S-HDAg
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