[NMR paper] NMR study of non-structural proteins-part I: (1)H, (13)C, (15)N backbone and side-chain resonance assignment of macro domain from Mayaro virus (MAYV).
Related ArticlesNMR study of non-structural proteins-part I: (1)H, (13)C, (15)N backbone and side-chain resonance assignment of macro domain from Mayaro virus (MAYV).
Biomol NMR Assign. 2014 Sep 13;
Authors: Melekis E, Tsika AC, Lichičre J, Chasapis CT, Margiolaki I, Papageorgiou N, Coutard B, Bentrop D, Spyroulias GA
Abstract
Macro domains are ADP-ribose-binding modules present in all eukaryotic organisms, bacteria and archaea. They are also found in non-structural proteins of several positive strand RNA viruses such as alphaviruses. Here, we report the high yield expression and preliminary structural analysis through solution NMR spectroscopy of the macro domain from New World Mayaro Alphavirus. The recombinant protein was well-folded and in a monomeric state. An almost complete sequence-specific assignment of its (1)H, (15)N and (13)C resonances was obtained and its secondary structure determined by TALOS+.
PMID: 25217003 [PubMed - as supplied by publisher]
[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] Backbone (1)H, (15)N, (13)C and side chain (13)C? NMR chemical shift assignment of murine interleukin-10.
Backbone (1)H, (15)N, (13)C and side chain (13)C? NMR chemical shift assignment of murine interleukin-10.
Backbone (1)H, (15)N, (13)C and side chain (13)C? NMR chemical shift assignment of murine interleukin-10.
Biomol NMR Assign. 2013 Aug 25;
Authors: Künze G, Theisgen S, Huster D
Abstract
Almost complete assignment of backbone (1)H, (13)C, (15)N and side chain (13)C? resonances for the immune-regulatory cytokine IL-10 is reported. The protein was overexpressed in Escherichia coli and was refolded from inclusion bodies. The point...
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08-29-2013 01:53 PM
[NMR paper] (1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus.
(1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus.
Related Articles (1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus.
Biomol NMR Assign. 2013 May 18;
Authors: Fonner BA, Tripet BP, Lui M, Zhu H, Lei B, Copié V
Abstract
Staphylococcus aureus is an opportunistic pathogen that...
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05-21-2013 02:34 PM
[NMR paper] Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain.
Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain.
Biomol NMR Assign. 2013 Jan 22;
Authors: Orbán-Németh Z, Henen MA, Geist L, Zerko S, Saxena S, Stanek J, Ko?mi?ski W, Propst F, Konrat R
Abstract
Microtubule-associated protein 1B (MAP1B) is a classical...
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02-03-2013 10:19 AM
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Biomol NMR Assign. 2011 Jun 7;
Authors: Wood K, Paz A, Dijkstra K, Scheek RM, Otten R, Silman I, Sussman JL, Mulder FA
Neuroligins act as heterophilic adhesion molecules at neuronal synapses. Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered. Here we...
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06-08-2011 11:30 AM
[NMR paper] Automated resonance assignment of proteins using heteronuclear 3D NMR. 2. Side chain
Automated resonance assignment of proteins using heteronuclear 3D NMR. 2. Side chain and sequence-specific assignment.
Related Articles Automated resonance assignment of proteins using heteronuclear 3D NMR. 2. Side chain and sequence-specific assignment.
J Chem Inf Comput Sci. 1997 May-Jun;37(3):467-77
Authors: Li KB, Sanctuary BC
A sequential assignment protocol for proteins was developed using heteronuclear 3D NMR. The protocol consists of an amino acid type recognition algorithm and a primary sequence mapping algorithm. The former measures...
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08-22-2010 03:31 PM
[NMR paper] Automated resonance assignment of proteins using heteronuclear 3D NMR. 2. Side chain
Automated resonance assignment of proteins using heteronuclear 3D NMR. 2. Side chain and sequence-specific assignment.
Related Articles Automated resonance assignment of proteins using heteronuclear 3D NMR. 2. Side chain and sequence-specific assignment.
J Chem Inf Comput Sci. 1997 May-Jun;37(3):467-77
Authors: Li KB, Sanctuary BC
A sequential assignment protocol for proteins was developed using heteronuclear 3D NMR. The protocol consists of an amino acid type recognition algorithm and a primary sequence mapping algorithm. The former measures...
NMR study of non-structural proteins-part I: (1)H, (13)C, (15)N backbone and side-chain resonance assignment of macro domain from Mayaro virus (MAYV).
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