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A fine balance of hydrophobic-electrostatic communication pathways in a pH-switching protein | Proceedings of the National Academy of Sciences - pnas.org
Jun 29, 2022 - 5:34 AM - by nmrlearner
nmrlearner's Avatar A fine balance of hydrophobic-electrostatic communication pathways in a pH-switching protein | Proceedings of the National Academy of Sciences - pnas.org

A fine balance of hydrophobic-electrostatic communication pathways in a pH-switching protein | Proceedings of the National Academy of Sciences pnas.org Read here
0 Replies | 1 Views
[NMR paper] 19F-NMR Unveils the Ligand-Induced Conformation of a Catalytically Inactive Twisted Homodimer of tRNA-Guanine Transglycosylase
Jun 29, 2022 - 5:34 AM - by nmrlearner
nmrlearner's Avatar 19F-NMR Unveils the Ligand-Induced Conformation of a Catalytically Inactive Twisted Homodimer of tRNA-Guanine Transglycosylase

Understanding the structural arrangements of protein oligomers can support the design of ligands that interfere with their function in order to develop new therapeutic concepts for disease treatment. Recent crystallographic studies have elucidated a novel twisted and functionally inactive form of the homodimeric enzyme tRNA-guanine transglycosylase (TGT), a putative target in the fight against shigellosis. Active-site ligands have been identified that stimulate the rearrangement of one monomeric...

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New insights of how HIV-1 assembles and incorporates Env protein - Mirage News
Jun 26, 2022 - 9:05 PM - by nmrlearner
nmrlearner's Avatar New insights of how HIV-1 assembles and incorporates Env protein - Mirage News

New insights of how HIV-1 assembles and incorporates Env protein Mirage News Read here
0 Replies | 10 Views
Study shows molecular details of HIV-1 assembly and viral envelope protein incorporation - News-Medical.Net
Jun 26, 2022 - 4:52 AM - by nmrlearner
nmrlearner's Avatar Study shows molecular details of HIV-1 assembly and viral envelope protein incorporation - News-Medical.Net

Study shows molecular details of HIV-1 assembly and viral envelope protein incorporation News-Medical.Net Read here
0 Replies | 12 Views
[NMR paper] Conformational Changes in Ff Phage Protein gVp upon Complexation with Its Viral Single-Stranded DNA Revealed Using Magic-Angle Spinning Solid-State NMR
Jun 24, 2022 - 11:45 PM - by nmrlearner
nmrlearner's Avatar Conformational Changes in Ff Phage Protein gVp upon Complexation with Its Viral Single-Stranded DNA Revealed Using Magic-Angle Spinning Solid-State NMR

Gene V protein (gVp) of the bacteriophages of the Ff family is a non-specific single-stranded DNA (ssDNA) binding protein. gVp binds to viral DNA during phage replication inside host Escherichia coli cells, thereby blocking further replication and signaling the assembly of new phage particles. gVp is a dimer in solution and in crystal form. A structural model of the complex between gVp and ssDNA was obtained via docking the free gVp to structures of short ssDNA segments and via the detection of...

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0 Replies | 13 Views
[NMR paper] DMSO-Quenched H/D-Exchange 2D NMR Spectroscopy and Its Applications in Protein Science
Jun 24, 2022 - 11:45 PM - by nmrlearner
nmrlearner's Avatar DMSO-Quenched H/D-Exchange 2D NMR Spectroscopy and Its Applications in Protein Science

Hydrogen/deuterium (H/D) exchange combined with two-dimensional (2D) NMR spectroscopy has been widely used for studying the structure, stability, and dynamics of proteins. When we apply the H/D-exchange method to investigate non-native states of proteins such as equilibrium and kinetic folding intermediates, H/D-exchange quenching techniques are indispensable, because the exchange reaction is usually too fast to follow by 2D NMR. In this article, we will describe the dimethylsulfoxide...

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[NMR paper] Interactions between S100A9 and Alpha-Synuclein: Insight from NMR Spectroscopy
Jun 24, 2022 - 11:45 PM - by nmrlearner
nmrlearner's Avatar Interactions between S100A9 and Alpha-Synuclein: Insight from NMR Spectroscopy

S100A9 is a pro-inflammatory protein that co-aggregates with other proteins in amyloid fibril plaques. S100A9 can influence the aggregation kinetics and amyloid fibril structure of alpha-synuclein (?-syn), which is involved in Parkinson's disease. Currently, there are limited data regarding their cross-interaction and how it influences the aggregation process. In this work, we analyzed this interaction using solution 19F and 2D ^(15)N-H HSQC NMR spectroscopy and studied the aggregation...

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