Mapping the Interactions between the NS4B and NS3 Proteins of Dengue Virus - Journal of Virology
Mapping the Interactions between the NS4B and NS3 Proteins of Dengue Virus - Journal of Virology
Mapping the Interactions between the NS4B and NS3 Proteins of Dengue Virus Journal of Virology
Using nuclear magnetic resonance (NMR), we found that the isolated cytoplasmic loop of NS4B is flexible, with a tendency to form a three-turn α-helix and two short β-strands. Upon binding to the NS3 helicase, 12 amino acids within the cytoplasmic loop ...
[NMR paper] Mapping substrate interactions of the human membrane-associated neuraminidase, NEU3, using STD NMR.
Mapping substrate interactions of the human membrane-associated neuraminidase, NEU3, using STD NMR.
Related Articles Mapping substrate interactions of the human membrane-associated neuraminidase, NEU3, using STD NMR.
Glycobiology. 2014 Oct 6;
Authors: Albohy A, Richards MR, Cairo CW
Abstract
Saturation transfer difference (STD) NMR is a powerful technique which can be used to investigate interactions between proteins and their substrates. The method identifies specific sites of interaction found on a small molecule ligand when in...
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[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).
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 Articles 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).
Biomol NMR Assign. 2014 Sep 13;
Authors: Melekis E, Tsika AC, Lichière J, Chasapis CT, Margiolaki I, Papageorgiou N, Coutard B, Bentrop D, Spyroulias GA
Abstract
Macro domains are ADP-ribose-binding modules present...
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09-14-2014 02:26 PM
[NMR paper] NMR analysis of a novel enzymatically-active unlinked Dengue NS2B-NS3 protease complex.
NMR analysis of a novel enzymatically-active unlinked Dengue NS2B-NS3 protease complex.
Related Articles NMR analysis of a novel enzymatically-active unlinked Dengue NS2B-NS3 protease complex.
J Biol Chem. 2013 Mar 19;
Authors: Kim YM, Gayen S, Kang C, Joy J, Huang Q, Chen AS, Wee JL, Ang MJ, Lim HA, Hung AW, Li R, Noble CG, Lee LT, Yip A, Wang QY, Chia CS, Hill J, Shi PY, Keller TH
Abstract
The dengue virus (DENV) is a mosquito-borne pathogen responsible for an estimated 100 million human infections annually. The viral genome encodes a...
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03-21-2013 02:58 PM
[NMR paper] Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble
Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations.
Related Articles Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations.
J Am Chem Soc. 2005 Jan 19;127(2):476-7
Authors: Dedmon MM, Lindorff-Larsen K, Christodoulou J, Vendruscolo M, Dobson CM
The intrinsically disordered protein alpha-synuclein plays a key role in the pathogenesis of Parkinson's disease (PD). We show here that the native state of alpha-synuclein...
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[NMR paper] Atomic mapping of the interactions between the antiviral agent cyanovirin-N and oligo
Atomic mapping of the interactions between the antiviral agent cyanovirin-N and oligomannosides by saturation-transfer difference NMR.
Related Articles Atomic mapping of the interactions between the antiviral agent cyanovirin-N and oligomannosides by saturation-transfer difference NMR.
Biochemistry. 2004 Nov 9;43(44):13926-31
Authors: Sandström C, Berteau O, Gemma E, Oscarson S, Kenne L, Gronenborn AM
The minimum oligosaccharide structure required for binding to the potent HIV-inactivating protein cyanovirin-N (CV-N) was determined by...
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11-24-2010 10:03 PM
[NMR paper] Epitope mapping of ligand-receptor interactions by diffusion NMR.
Epitope mapping of ligand-receptor interactions by diffusion NMR.
Related Articles Epitope mapping of ligand-receptor interactions by diffusion NMR.
J Am Chem Soc. 2002 Aug 28;124(34):9984-5
Authors: Yan J, Kline AD, Mo H, Zartler ER, Shapiro MJ
A novel method based on diffusion NMR for the epitope mapping of ligand binding is presented. The intermolecular NOE builds up during a long diffusion period and creates a deviation from the linearity. The ligand proton nearest the protein generates the strongest NOE from protein during the diffusion...
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[NMR paper] Interactions of a vesicular stomatitis virus G protein fragment with phosphatidylseri
Interactions of a vesicular stomatitis virus G protein fragment with phosphatidylserine: NMR and fluorescence studies.
Related Articles Interactions of a vesicular stomatitis virus G protein fragment with phosphatidylserine: NMR and fluorescence studies.
Biochim Biophys Acta. 1998 Dec 9;1415(1):101-13
Authors: Hall MP, Burson KK, Huestis WH
The interaction of a 19 amino acid vesicular stomatitis virus G protein fragment (GTWLNPGFPPQSCGYATVT) with phosphatidylserine-containing model membranes was investigated using solution-phase 1d and 2d 1H...
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11-17-2010 11:15 PM
Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)
Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)
David S Burz, Kaushik Dutta, David Cowburn & Alexander Shekhtman
We describe a high-throughput in-cell nuclear magnetic resonance (NMR)-based method for mapping the structural changes that accompany protein-protein interactions (STINT-NMR). The method entails sequentially expressing two (or more) proteins within a single bacterial cell in a time-controlled manner and monitoring the protein interactions using in-cell NMR spectroscopy. The resulting spectra provide a complete titration of the interaction and define...