NMR is a powerful tool for characterizing intermolecular interactions at atomic resolution. However, the nature of the complex interactions of membrane-binding proteins makes it difficult to elucidate the interaction mechanisms. Here, we demonstrated that structural and thermodynamic analyses using solution NMR spectroscopy and isothermal titration calorimetry (ITC) can clearly detect a specific interaction between the pleckstrin homology (PH) domain of ceramide transport protein (CERT) and...
[NMR paper] Multi-site binding of epigallocatechin gallate to human serum albumin measured by NMR and isothermal titration calorimetry.
Multi-site binding of epigallocatechin gallate to human serum albumin measured by NMR and isothermal titration calorimetry.
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Biosci Rep. 2017 Jun 30;37(3):
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[NMR paper] Use of Fluorine Pseudocontact Shifts to Characterize the Protein-Ligand Interaction Mode in the Limit of NMR Intermediate Exchange.
Use of Fluorine Pseudocontact Shifts to Characterize the Protein-Ligand Interaction Mode in the Limit of NMR Intermediate Exchange.
Use of Fluorine Pseudocontact Shifts to Characterize the Protein-Ligand Interaction Mode in the Limit of NMR Intermediate Exchange.
Angew Chem Int Ed Engl. 2017 Aug 28;:
Authors: Gao J, Liang E, Ma R, Li F, Liu Y, Liu J, Jiang L, Li C, Dai H, Wu J, Su X, He W, Ruan K
Abstract
The characterization of protein-ligand interaction modes becomes recalcitrant in the NMR intermediate exchange regime as the...
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08-29-2017 05:35 PM
[NMR paper] Use of Fluorine Pseudocontact Shifts to Characterize the Protein-Ligand Interaction Mode in the Limit of NMR Intermediate Exchange
Use of Fluorine Pseudocontact Shifts to Characterize the Protein-Ligand Interaction Mode in the Limit of NMR Intermediate Exchange
The characterization of protein-ligand interaction modes becomes recalcitrant in the NMR intermediate exchange regime as the interface resonances are broadened beyond detection. Here, we determined the 19F low-populated bound-state pseudocontact shifts (PCSs) of mono- and di-fluorinated inhibitors of the BRM bromodomain using a highly-skewed protein/ligand ratio. The bound-state 19F PCSs were retrieved from 19F chemical exchange saturation transfer (CEST) in...
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[NMR paper] Proton-Detected NMR Spectroscopy of Nanodisc-Embedded Membrane Proteins: MAS Solid-State vs. Solution-State Methods.
Proton-Detected NMR Spectroscopy of Nanodisc-Embedded Membrane Proteins: MAS Solid-State vs. Solution-State Methods.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Proton-Detected NMR Spectroscopy of Nanodisc-Embedded Membrane Proteins: MAS Solid-State vs. Solution-State Methods.
J Phys Chem B. 2017 Jul 24;:
Authors: Lakomek NA, Frey L, Bibow S, Böckmann A, Riek R, Meier BH
Abstract
The structural and dynamical characterization of membrane proteins...
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Using Isothermal Titration Calorimetry for Biophysical Characterization of Chromatin-Binding Proteins - News-Medical.net
Using Isothermal Titration Calorimetry for Biophysical Characterization of Chromatin-Binding Proteins - News-Medical.net
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Using Isothermal Titration Calorimetry for Biophysical Characterization of Chromatin-Binding Proteins
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Structural studies like nuclear magnetic resonance (NMR) and X-ray crystallography provide additional validation and characterization. This article describes the...
[NMR paper] Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.
Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.
Related Articles Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.
J Biol Chem. 2014 Aug 13;
Authors: Meneses E, Mittermaier A
Abstract
Much of our knowledge of protein binding pathways is derived from extremely stable complexes that interact very tightly, with lifetimes of hours to days. Much less is known about...
A hybrid strategy combining solution NMR spectroscopy and isothermal titration calorimetry to characterize protein-nanodisc interaction
Linear Mode
