[NMR paper] Deciphering the Dynamic Interaction Profile of an Intrinsically Disordered Protein by NMR Exchange Spectroscopy.
Deciphering the Dynamic Interaction Profile of an Intrinsically Disordered Protein by NMR Exchange Spectroscopy.
Deciphering the Dynamic Interaction Profile of an Intrinsically Disordered Protein by NMR Exchange Spectroscopy.
J Am Chem Soc. 2017 Dec 25;:
Authors: Delaforge E, Kragelj J, Tengo L, Palencia A, Milles S, Bouvignies G, Salvi N, Blackledge M, Jensen MR
Abstract
Intrinsically disordered proteins (IDPs) display a large number of interaction modes including folding-upon-binding, binding without major structural...
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12-26-2017 11:16 AM
[NMR paper] The thermodynamic basis of the fuzzy interaction of an intrinsically disordered protein
The thermodynamic basis of the fuzzy interaction of an intrinsically disordered protein
Many intrinsically disordered proteins (IDP) that fold upon binding retain conformational heterogeneity in IDP-target complexes. The thermodynamics of such fuzzy interactions is poorly understood. Here we introduce a thermodynamic framework, based on analysis of ITC and CD spectroscopy data, that provides experimental description of IDP association in terms of folding and binding contributions which can be predicted using sequence folding propensities and molecular modeling. We show how IDP can...
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09-15-2017 08:41 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.
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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08-29-2017 01:33 AM
[NMR paper] Structure and dynamics of an intrinsically disordered protein region that partially folds upon binding by chemical-exchange NMR.
Structure and dynamics of an intrinsically disordered protein region that partially folds upon binding by chemical-exchange NMR.
Related Articles Structure and dynamics of an intrinsically disordered protein region that partially folds upon binding by chemical-exchange NMR.
J Am Chem Soc. 2017 Aug 07;:
Authors: Charlier C, Bouvignies G, Pelupessy P, Walrant A, Marquant R, Kozlov M, De Ioannes P, Bolik-Coulon N, Sagan S, Cortes P, Aggarwal AK, Carlier L, Ferrage F
Abstract
Many intrinsically disordered proteins (IDPs) and protein...
Dynamic UltraFast 2D EXchange SpectroscopY (UF-EXSY) of hyperpolarized substrates
From The DNP-NMR Blog:
Dynamic UltraFast 2D EXchange SpectroscopY (UF-EXSY) of hyperpolarized substrates
Leon Swisher, C., et al., Dynamic UltraFast 2D EXchange SpectroscopY (UF-EXSY) of hyperpolarized substrates. J Magn Reson, 2015. 257: p. 102-9.
http://www.ncbi.nlm.nih.gov/pubmed/26117655
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09-10-2015 01:10 AM
[NMR paper] Dynamics of the Intrinsically Disordered C-Terminal Domain of the Nipah Virus Nucleoprotein and Interaction with the X Domain of the Phosphoprotein as Unveiled by NMR Spectroscopy.
Dynamics of the Intrinsically Disordered C-Terminal Domain of the Nipah Virus Nucleoprotein and Interaction with the X Domain of the Phosphoprotein as Unveiled by NMR Spectroscopy.
Related Articles Dynamics of the Intrinsically Disordered C-Terminal Domain of the Nipah Virus Nucleoprotein and Interaction with the X Domain of the Phosphoprotein as Unveiled by NMR Spectroscopy.
Chembiochem. 2014 Dec 9;
Authors: Baronti L, Erales J, Habchi J, Felli IC, Pierattelli R, Longhi S
Abstract
We provide an atomic-resolution description...
Decipheringthe Dynamic Interaction Profile of anIntrinsically Disordered Protein by NMR Exchange Spectroscopy
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