pUL69 of Human Cytomegalovirus Recruits the Cellular Protein Arginine ... - Journal of Virology
pUL69 of Human Cytomegalovirus Recruits the Cellular Protein Arginine ... - Journal of Virology
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pUL69 of Human Cytomegalovirus Recruits the Cellular Protein Arginine ...
Journal of Virology
Remarkably, nuclear magnetic resonance (NMR) analyses revealed the same α-helical structures for pUL69 sequences encoding either the wild type R1/R2 boxes or a UAP56/PRMT6 binding-deficient derivative, thereby excluding the possibility that R/A ...
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08-20-2015 05:44 AM
Determinants of Dengue Virus NS4A Protein Oligomerization - Journal of Virology
Determinants of Dengue Virus NS4A Protein Oligomerization - Journal of Virology
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Determinants of Dengue Virus NS4A Protein Oligomerization
Journal of Virology
Nuclear magnetic resonance (NMR) analysis of NS4A amino acids 17 to 80 suggests that residues L31, L52, E53, G66, and G67 could participate in oligomerization. Ala substitution for 15 flavivirus conserved NS4A residues revealed that these amino acids ...
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05-16-2015 01:45 PM
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
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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 ...
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03-14-2015 06:49 AM
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
<img alt="" height="1" width="1">
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 ...
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03-10-2015 07:22 PM
â??Spaghetti-likeâ?? Arms of Herpes Virus Could Be a Therapeutic Target for Kaposi ... - BioNews Texas
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BioNews Texas
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â??Spaghetti-likeâ?? Arms of Herpes Virus Could Be a Therapeutic Target for Kaposi ...
BioNews Texas
The researchers examined how a monkey herpes virus binds with other large molecules, such as cellular proteins, in the host cell by using a technique called NMR (Nuclear Magnetic Resonance), which can visualize the structure of molecules at the ...
â??Spaghetti-likeâ?? Arms of Herpes Virus Could Be a...
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02-19-2014 12:07 AM
Siderocalin Q83 exhibits differential slow dynamics upon ligand binding
Siderocalin Q83 exhibits differential slow dynamics upon ligand binding
Abstract Siderocalin Q83 is a small soluble protein that has the ability to bind two different ligands (enterobactin and arachidonic acid) simultaneously in two distinct binding sites. Here we report that Q83 exhibits an intriguing dynamic behavior. In its free form, the protein undergoes significant micro-to-millisecond dynamics. When binding arachidonic acid, the motions of the arachidonic acid binding site are quenched while the dynamics at the enterobactin binding site increases. Reciprocally, enterobactin...
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09-30-2011 08:01 PM
[NMR paper] NMR assignment of the vaccinia virus envelope protein A27L.
NMR assignment of the vaccinia virus envelope protein A27L.
Related Articles NMR assignment of the vaccinia virus envelope protein A27L.
J Biomol NMR. 2005 Jun;32(2):178
Authors: Chu FI, Ho Y, Tzou DL
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11-25-2010 08:21 PM
[NMR paper] Structural analysis of the extracellular domain of vaccinia virus envelope protein, A
Structural analysis of the extracellular domain of vaccinia virus envelope protein, A27L, by NMR and CD spectroscopy.
Related Articles Structural analysis of the extracellular domain of vaccinia virus envelope protein, A27L, by NMR and CD spectroscopy.
J Biol Chem. 2002 Jun 7;277(23):20949-59
Authors: Lin TH, Chia CM, Hsiao JC, Chang W, Ku CC, Hung SC, Tzou DL
This study presents the molecular structure of the extracellular domain of vaccinia virus envelope protein, A27L, determined by NMR and CD spectroscopy. A recombinant protein, eA27L-aa,...