Protein plasticity and dynamics are important aspects of their function. Here we use solid-state NMR to experimentally characterize the dynamics of the 3.5 MDa hepatitis B virus (HBV) capsid, assembled from 240 copies of the Cp149 core protein. We measure both T (1) and T (1?) relaxation times, which we use to establish detectors on the nanosecond and microsecond timescale. We compare our results to those from a 1 microsecond all-atom Molecular Dynamics (MD) simulation trajectory for the capsid....
[NMR paper] Dimer organization of membrane-associated NS5A of hepatitis C virus as determined by highly sensitive*1H-detected solid-state NMR.
Dimer organization of membrane-associated NS5A of hepatitis C virus as determined by highly sensitive*1H-detected solid-state NMR.
Related Articles Dimer organization of membrane-associated NS5A of hepatitis C virus as determined by highly sensitive*1H-detected solid-state NMR.
Angew Chem Int Ed Engl. 2020 Nov 18;:
Authors: Jirasko V, Lends A, Lakomek NA, Fogeron ML, Weber M, Malär A, Penzel S, Bartenschlager R, Meier BH, Böckmann A
Abstract
The Hepatitis C virus nonstructural protein 5A (NS5A) is a membrane-associated protein...
[NMR paper] Non-uniformly sampled rare-spin 4D solid state NMR experiments: assignment and characterization of IKe phage capsid.
Non-uniformly sampled rare-spin 4D solid state NMR experiments: assignment and characterization of IKe phage capsid.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7388-69-wiley-full-text.png Related Articles Non-uniformly sampled rare-spin 4D solid state NMR experiments: assignment and characterization of IKe phage capsid.
Magn Reson Chem. 2020 Jun 30;:
Authors: Porat G, Lusky O, Dayan N, Goldbourt A
Abstract
An important step in the process of protein research by NMR is the...
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07-01-2020 07:32 PM
[ASAP] Dynamics of Zika Virus Capsid Protein in Solution: The Properties and Exposure of the Hydrophobic Cleft Are Controlled by the a-Helix 1 Sequence
Dynamics of Zika Virus Capsid Protein in Solution: The Properties and Exposure of the Hydrophobic Cleft Are Controlled by the a-Helix 1 Sequence
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.9b00194/20190506/images/medium/bi-2019-00194d_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.9b00194
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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05-07-2019 05:41 AM
[NMR paper] Solid-state [13C-15N] NMR resonance assignment of hepatitis B virus core protein.
Solid-state NMR resonance assignment of hepatitis B virus core protein.
Related Articles Solid-state NMR resonance assignment of hepatitis B virus core protein.
Biomol NMR Assign. 2018 Feb 16;:
Authors: Lecoq L, Wang S, Wiegand T, Bressanelli S, Nassal M, Meier BH, Böckmann A
Abstract
Each year, nearly 900,000 deaths are due to serious liver diseases caused by chronic hepatitis B virus infection. The viral particle is composed of an outer envelope and an inner icosahedral nucleocapsid formed by multiple dimers of a ~ 20*kDa...
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02-18-2018 05:54 AM
Hepatitis C Virus: NMR reveals replication essentials
Hepatitis C Virus: NMR reveals replication essentials
http://www.spectroscopynow.com/common/images/thumbnails/14d9ad23f5d.jpgNMR spectroscopy and other techniques underpin research at the University of Southampton into how changes in the cell membrane play a pivotal role in how the Hepatitis C virus replicates.
Read the rest at Spectroscopynow.com
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06-01-2015 02:52 AM
[NMR paper] Insights into the Structure and Dynamics of Measles Virus Nucleocapsids by (1)H-detected Solid-state NMR.
Insights into the Structure and Dynamics of Measles Virus Nucleocapsids by (1)H-detected Solid-state NMR.
Related Articles Insights into the Structure and Dynamics of Measles Virus Nucleocapsids by (1)H-detected Solid-state NMR.
Biophys J. 2014 Aug 19;107(4):941-946
Authors: Barbet-Massin E, Felletti M, Schneider R, Jehle S, Communie G, Martinez N, Jensen MR, Ruigrok RW, Emsley L, Lesage A, Blackledge M, Pintacuda G
Abstract
(1)H-detected solid-state nuclear magnetic resonance (NMR) experiments are recorded on both intact...
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08-21-2014 06:43 PM
[NMR paper] Global fold and backbone dynamics of the hepatitis C virus E2 glycoprotein transmembrane domain determined by NMR.
Global fold and backbone dynamics of the hepatitis C virus E2 glycoprotein transmembrane domain determined by NMR.
Related Articles Global fold and backbone dynamics of the hepatitis C virus E2 glycoprotein transmembrane domain determined by NMR.
Biochim Biophys Acta. 2014 Aug 7;
Authors: Shalom-Elazari H, Zazrin-Greenspon H, Shaked H, Chill JH
Abstract
E1 and E2 are two hepatitis C viral envelope glycoproteins that assemble into a heterodimer that is essential for membrane fusion and penetration into the target cell. Both...
Experimental Characterization of the Hepatitis B Virus Capsid Dynamics by Solid-State NMR
Linear Mode
