The cellular environment is a complex and crowded space, with organelles, compartments and multitudes of molecules engaged in intricate networks of communication that modulate binary protein-ligand/protein interactions. As a result, it is becoming increasingly appreciated that evaluations of protein-drug binding should be carried out in the native cellular environment. Here, we present a proof-of-concept study where we measured the lifetime (1/k(off)) of a protein-drug complex in human cells by...
[ASAP] Direct Expression of Fluorinated Proteins in Human Cells for 19F In-Cell NMR Spectroscopy
Direct Expression of Fluorinated Proteins in Human Cells for 19F In-Cell NMR Spectroscopy
Lan B. T. Pham, Azzurra Costantino, Letizia Barbieri, Vito Calderone, Enrico Luchinat, and Lucia Banci
https://pubs.acs.org/cms/10.1021/jacs.2c12086/asset/images/medium/ja2c12086_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.2c12086
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01-06-2023 08:16 PM
[NMR paper] Direct Expression of Fluorinated Proteins in Human Cells for 19F In-Cell NMR Spectroscopy
Direct Expression of Fluorinated Proteins in Human Cells for 19F In-Cell NMR Spectroscopy
In-cell NMR spectroscopy is a powerful approach to study protein structure and function in the native cellular environment. It provides precious insights into the folding, maturation, interactions, and ligand binding of important pharmacological targets directly in human cells. However, its widespread application is hampered by the fact that soluble globular proteins often interact with large cellular components, causing severe line broadening in conventional heteronuclear NMR experiments....
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01-06-2023 08:16 PM
[NMR paper] Quantifying the thermodynamics of protein unfolding using 2D NMR spectroscopy
Quantifying the thermodynamics of protein unfolding using 2D NMR spectroscopy
A topic that has attracted considerable interest in recent years is the possibility to perform thermodynamic studies of proteins directly in-cell or in complex environments which mimic the cellular interior. Nuclear magnetic resonance (NMR) could be an attractive technique for these studies but its applicability has so far been limited by technical issues. Here, we demonstrate that 2D NMR methods can be successfully applied to measure thermodynamic parameters provided that a suitable choice of...
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03-16-2021 06:18 AM
[NMR paper] Observation of nucleic acids inside living human cells by in-cell NMR spectroscopy.
Observation of nucleic acids inside living human cells by in-cell NMR spectroscopy.
Observation of nucleic acids inside living human cells by in-cell NMR spectroscopy.
Biophys Physicobiol. 2020;17:36-41
Authors: Yamaoki Y, Nagata T, Sakamoto T, Katahira M
Abstract
The intracellular environment is highly crowded with biomacromolecules such as proteins and nucleic acids. Under such conditions, the structural and biophysical features of nucleic acids have been thought to be different from those in vitro. To obtain high-resolution...
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10-29-2020 10:21 AM
Hyperpolarized singlet lifetimes of pyruvate in human blood and in the mouse
From The DNP-NMR Blog:
Hyperpolarized singlet lifetimes of pyruvate in human blood and in the mouse
Marco-Rius, I., et al., Hyperpolarized singlet lifetimes of pyruvate in human blood and in the mouse. NMR Biomed, 2013. 26(12): p. 1696-704.
http://www.ncbi.nlm.nih.gov/pubmed/23946252
Quantifying protein-drug lifetimes in human cells by (19)F NMR spectroscopy
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