[Recent progress in nuclear magnetic resonance spectrum for drug research and development]

Related Concept Videos

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue07:40

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue

Here, we present a protocol detailing the acquisition, processing, and analysis of a series of NMR experiments aimed at characterizing protein-glycan interactions in solution. Most common ligand-based and protein-based methodologies are outlined, which undoubtedly contribute to the fields of structural glycobiology and molecular recognition studies.
1.9K
Nuclear Magnetic Resonance (NMR) Spectroscopy10:08

Nuclear Magnetic Resonance (NMR) Spectroscopy

Source: Laboratory of Dr. Henrik Sundén – Chalmers University of Technology
256.4K
Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy07:02

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy

The present protocol describes the preparation and quantitative measurement of free and protein-bound arginine and methyl-arginines by 1H-NMR...
1.8K
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

We describe here a method to identify multiple phosphorylations of an intrinsically disordered protein by Nuclear Magnetic Resonance Spectroscopy (NMR), using Tau protein as a case study. Recombinant Tau is isotopically enriched and modified in vitro by a kinase prior to data acquisition and...
19.4K
Nuclear Magnetic Resonance Spectroscopy to Identify Multiple Phosphorylations in Proteins04:47

Nuclear Magnetic Resonance Spectroscopy to Identify Multiple Phosphorylations in Proteins

This video demonstrates the use of nuclear magnetic resonance spectroscopy (NMR) techniques to identify multiple phosphorylations in a protein. The phosphorylation of a protein at specific amino acid causes the deshielding of the neighboring amide hydrogen, which generates the spectral...
774
Nuclear Magnetic Resonance to Study Atomic Level Protein-Protein Interactions06:05

Nuclear Magnetic Resonance to Study Atomic Level Protein-Protein Interactions

This video describes the nuclear magnetic resonance spectroscopy technique to study protein-protein interactions between 15N-labeled wild-type and mutant envoplakin proteins and the unlabeled vimentin protein. The successful interaction between wild-type envoplakin and vimentin leads to extensive line broadening and peak disappearance in the NMR spectra, whereas the absence of an interaction between the mutated envoplakin and vimentin results in well-resolved peaks in the NMR...
748