[NMR paper] NMR methods for exploring 'dark' states in ligand binding and protein-protein interactions
NMR methods for exploring 'dark' states in ligand binding and protein-protein interactions
A survey, primarily based on work in the authors' laboratory during the last 10 years, is provided of recent developments in NMR studies of exchange processes involving protein-ligand and protein-protein interactions. We start with a brief overview of the theoretical background of Dark state Exchange Saturation Transfer (DEST) and lifetime line-broadening (?R(2)) NMR methodology. Some limitations of the DEST/?R(2) methodology in applications to molecular systems with intermediate molecular...
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03-18-2022 12:01 AM
[NMR paper] Investigation of protein-ligand complexes by ligand-based NMR methods
Investigation of protein-ligand complexes by ligand-based NMR methods
Molecular recognition is at the base of all biological events and its knowledge at atomic level is pivotal in the development of new drug design approaches. NMR spectroscopy is one of the most widely used technique to detect and characterize transient ligand-receptor interactions in solution. In particular, ligand-based NMR approaches, including NOE-based NMR techniques, diffusion experiments and relaxation methods, are excellent tools to investigate how ligands interact with their receptors....
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04-18-2021 11:34 AM
[NMR paper] Exploring Weak Ligand-Protein Interactions by Long-Lived NMR States : Improved Contrast in Fragment-Based Drug Screening.
Exploring Weak Ligand-Protein Interactions by Long-Lived NMR States : Improved Contrast in Fragment-Based Drug Screening.
Related Articles Exploring Weak Ligand-Protein Interactions by Long-Lived NMR States : Improved Contrast in Fragment-Based Drug Screening.
Angew Chem Int Ed Engl. 2014 Sep 4;
Authors: Buratto R, Mammoli D, Chiarparin E, Williams G, Bodenhausen G
Abstract
Ligands that have an affinity for protein targets can be screened very effectively by exploiting favorable properties of long-lived states (LLS) in NMR...
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09-10-2014 11:24 AM
[NMR paper] (19) F NMR as a Probe of Ligand Interactions with the iNOS Binding site of SPRY-Domain Containing SOCS Box Protein 2.
(19) F NMR as a Probe of Ligand Interactions with the iNOS Binding site of SPRY-Domain Containing SOCS Box Protein 2.
(19) F NMR as a Probe of Ligand Interactions with the iNOS Binding site of SPRY-Domain Containing SOCS Box Protein 2.
Chem Biol Drug Des. 2014 May 9;
Authors: Leung EW, Yagi H, Harjani JR, Mulcair MD, Scanlon MJ, Baell JB, Norton RS
Abstract
SPRY domain-containing SOCS box protein 2 (SPSB2) regulates inducible nitric oxide synthase (iNOS) by targeting it for proteasomal degradation. Inhibiting this interaction...
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05-13-2014 03:11 PM
Research and Markets: Protein-Ligand Interactions. Methods and Principles in ... - Business Wire (press release)
Research and Markets: Protein-Ligand Interactions. Methods and Principles in ... - Business Wire (press release)
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Research and Markets: Protein-Ligand Interactions. Methods and Principles in ...
Business Wire (press release)
The first part provides a basic understanding of the factors governing protein-ligand interaction, followed by a comparison of the four key experimental methods (calorimetry, surface plasmon resonance, NMR and X-ray crystallography) used in generating ...
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08-29-2012 04:31 PM
Exploring NMR ensembles of calcium binding proteins: perspectives to design inhibitors of protein-protein interactions.
Exploring NMR ensembles of calcium binding proteins: perspectives to design inhibitors of protein-protein interactions.
Exploring NMR ensembles of calcium binding proteins: perspectives to design inhibitors of protein-protein interactions.
BMC Struct Biol. 2011 May 12;11(1):24
Authors: Isvoran A, Badel A, Craescu CT, Miron S, Miteva MA
ABSTRACT: BACKGROUND: Disrupting protein-protein interactions by small organic molecules is nowadays a promising strategy employed to block protein targets involved in different pathologies. However, structural...
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05-17-2011 06:21 PM
[NMR paper] Probing the binding entropy of ligand-protein interactions by NMR.
Probing the binding entropy of ligand-protein interactions by NMR.
Related Articles Probing the binding entropy of ligand-protein interactions by NMR.
Chembiochem. 2005 Sep;6(9):1585-91
Authors: Homans SW