[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...
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11-20-2020 09:24 AM
Real-Time In-Cell Nuclear Magnetic Resonance: Ribosome-TargetedAntibiotics Modulate Quinary Protein Interactions
Real-Time In-Cell Nuclear Magnetic Resonance: Ribosome-TargetedAntibiotics Modulate Quinary Protein Interactions
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00938/20180108/images/medium/bi-2017-00938t_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00938
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01-09-2018 09:41 AM
[NMR paper] Real Time In-cell NMR: Ribosome Targeted Antibiotics Modulate Quinary Protein Interactions.
Real Time In-cell NMR: Ribosome Targeted Antibiotics Modulate Quinary Protein Interactions.
Real Time In-cell NMR: Ribosome Targeted Antibiotics Modulate Quinary Protein Interactions.
Biochemistry. 2017 Dec 21;:
Authors: Breindel LM, DeMott CM, Burz DS, Shekhtman A
Abstract
It is not well understood how ribosome antibiotics affect a wide range of biochemical pathways; changes in RNA-mediated protein quinary interactions and consequent activity inside the crowded cytosol may provide one possible mechanism. We developed real-time...
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12-22-2017 07:55 PM
[NMR paper] Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR.
Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR.
Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR.
Nat Protoc. 2018 Jan;13(1):79-98
Authors: Hagn F, Nasr ML, Wagner G
Abstract
Suitable membrane mimetics are crucial to the performance of structural and functional studies of membrane proteins. Phospholipid nanodiscs (formed when a membrane scaffold protein encircles a small portion of a lipid bilayer) have...
[NMR paper] Fluoroacetamide Moieties as NMR Probes for molecular recognition of GlcNAc-containing sugars: Modulation of the CH-? Stacking Interactions by Different Fluorination Patterns.
Fluoroacetamide Moieties as NMR Probes for molecular recognition of GlcNAc-containing sugars: Modulation of the CH-? Stacking Interactions by Different Fluorination Patterns.
Fluoroacetamide Moieties as NMR Probes for molecular recognition of GlcNAc-containing sugars: Modulation of the CH-? Stacking Interactions by Different Fluorination Patterns.
Chemistry. 2017 Jan 26;:
Authors: Unione L, Alcalá M, Echeverria B, Serna S, Ardá A, Franconetti A, Cañada J, Diercks T, Reichardt N, Jimenez-Barbero J
Abstract
We herein propose the...
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01-27-2017 12:04 PM
Drugs Modulate Interactions between the First Nucleotide-BindingDomain and the Fourth Cytoplasmic Loop of Human P-Glycoprotein
Drugs Modulate Interactions between the First Nucleotide-BindingDomain and the Fourth Cytoplasmic Loop of Human P-Glycoprotein
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00233/20160511/images/medium/bi-2016-00233f_0003.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00233
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