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[NMR paper] High-Efficiency Trifluoromethyl-Methionine Incorporation into Cyclophilin A by Cell-Free Synthesis for 19F NMR Studies
Nov 22, 2024 - 12:06 AM - by nmrlearner
nmrlearner's Avatar High-Efficiency Trifluoromethyl-Methionine Incorporation into Cyclophilin A by Cell-Free Synthesis for 19F NMR Studies

Fluorine-19 NMR spectroscopy has emerged as a powerful tool for studying protein structure, dynamics, and interactions. Of particular interest is the exploitation of trifluoromethyl (tfm) groups, given their high sensitivity and superior transverse relaxation properties, compared to single fluorine atoms. However, biosynthetic incorporation of tfm-bearing amino acids remains challenging due to cytotoxicity and incompatibility with natural tRNA synthetases. Here, we report on overcoming this...

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0 Replies | 9 Views
1H Nuclear Magnetic Resonance Spectroscopy-Based Methods for the Quantification of Proteins in Urine - ACS Publications
Nov 21, 2024 - 12:00 PM - by nmrlearner
nmrlearner's Avatar 1H Nuclear Magnetic Resonance Spectroscopy-Based Methods for the Quantification of Proteins in Urine ACS Publications
1H Nuclear Magnetic Resonance Spectroscopy-Based Methods for the Quantification of Proteins in Urine - ACS Publications
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0 Replies | 24 Views
[NMR paper] Radio frequency gradient enhanced diffusion-edited semi-solid state NMR spectroscopy for detailed structural characterization of chemically modified hyaluronic acid hydrogels
Nov 20, 2024 - 5:31 PM - by nmrlearner
nmrlearner's Avatar Radio frequency gradient enhanced diffusion-edited semi-solid state NMR spectroscopy for detailed structural characterization of chemically modified hyaluronic acid hydrogels

Applications of functionalized hyaluronic acid (HA) hydrogels for numerous biomedical applications requires their detailed structural characterization. Since these materials are prepared by multistep chemical modifications in the solid phase and not amenable to characterization by standard analytical tools, we employed high-resolution solid-state NMR spectroscopy to gain detailed insights into the structures of the functionalized HA hydrogels. Divinyl sulfone crosslinked HA hydrogels were...

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0 Replies | 74 Views
[NMR paper] Comparative analysis of polysaccharide and cell wall structure in Aspergillus nidulans and Aspergillus fumigatus by solid-state NMR
Nov 20, 2024 - 5:23 AM - by nmrlearner
nmrlearner's Avatar Comparative analysis of polysaccharide and cell wall structure in Aspergillus nidulans and Aspergillus fumigatus by solid-state NMR

Invasive aspergillosis poses a significant threat to immunocompromised patients, leading to high mortality rates associated with these infections. Targeting the biosynthesis of cell wall carbohydrates is a promising strategy for antifungal drug development and will be advanced by a molecular-level understanding of the native structures of polysaccharides within their cellular context. Solid-state NMR spectroscopy has recently provided detailed insights into the cell wall organization of...

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0 Replies | 52 Views
Investigation of Protein Therapeutics in Frozen Conditions Using DNP MAS NMR: A Study on Pembrolizumab - ACS Publications
Nov 19, 2024 - 3:00 PM - by nmrlearner
nmrlearner's Avatar Investigation of Protein Therapeutics in Frozen Conditions Using DNP MAS NMR: A Study on Pembrolizumab - ACS Publications

Investigation of Protein Therapeutics in Frozen Conditions Using DNP MAS NMR: A Study on Pembrolizumab ACS Publications Read here
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[NMR paper] Investigation of Protein Therapeutics in Frozen Conditions Using DNP MAS NMR: A Study on Pembrolizumab
Nov 18, 2024 - 9:13 PM - by nmrlearner
nmrlearner's Avatar Investigation of Protein Therapeutics in Frozen Conditions Using DNP MAS NMR: A Study on Pembrolizumab

The success of modern biopharmaceutical products depends on enhancing the stability of protein therapeutics. Freezing and thawing, which are common thermal stresses encountered throughout the lifecycle of drug substances, spanning protein production, formulation design, manufacturing, storage, and shipping, can impact this stability. Understanding the physicochemical and molecular behaviors of components in biological drug products at temperatures relevant to manufacturing and shipping is...

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0 Replies | 26 Views
[NMR paper] NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
Nov 18, 2024 - 9:13 PM - by nmrlearner
nmrlearner's Avatar NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Nuclear magnetic resonance (NMR) spectroscopy allows studying proteins in solution and under physiological temperatures. Frequently, either the amide groups of the protein backbone or the methyl groups in side chains are used as reporters of structural dynamics in proteins. A structural dynamics study of the protein backbone of globular proteins on ^(15)N labeled and fully protonated samples usually works well for proteins with a molecular weight of up to 50 kDa. When side chain deuteration in...

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0 Replies | 24 Views
[NMR paper] Structural Model of Bacteriophage P22 Scaffolding Protein in a Procapsid by Magic-Angle Spinning NMR
Nov 18, 2024 - 9:13 PM - by nmrlearner
nmrlearner's Avatar Structural Model of Bacteriophage P22 Scaffolding Protein in a Procapsid by Magic-Angle Spinning NMR

Icosahedral dsDNA viruses such as the tailed bacteriophages and herpesviruses have a conserved pathway to virion assembly that is initiated from a scaffolding protein driven procapsid formation. The dsDNA is actively packaged into procapsids, which undergo complex maturation reactions to form infectious virions. In bacteriophage P22, scaffolding protein (SP) directs the assembly of coat proteins into procapsids that have a T=7 icosahedral arrangement, en route to the formation of the mature P22...

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0 Replies | 27 Views
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