Many human proteins possess intrinsically disordered regions containing consecutive aspartate or glutamate residues ("D/E repeats"). Approximately half of them are DNA/RNA-binding proteins. In this study, using nuclear magnetic resonance (NMR) spectroscopy, we investigated the electrostatic properties of D/E repeats and their influence on folded domains within the same protein. Local electrostatic potentials were directly measured for the HMGB1 protein, its isolated D/E repeats, and DNA-binding...
[NMR paper] Obtaining Hydrodynamic Radii of Intrinsically Disordered Protein Ensembles by Pulsed Field Gradient NMR Measurements.
Obtaining Hydrodynamic Radii of Intrinsically Disordered Protein Ensembles by Pulsed Field Gradient NMR Measurements.
Related Articles Obtaining Hydrodynamic Radii of Intrinsically Disordered Protein Ensembles by Pulsed Field Gradient NMR Measurements.
Methods Mol Biol. 2020;2141:285-302
Authors: Leeb S, Danielsson J
Abstract
In the disordered state, a protein exhibits a high degree of structural freedom, in both space and time. For an ensemble of disordered or unfolded proteins, this means that the ensemble comprises a high...
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[NMR paper] Protein-excipient interactions evaluated via NMR studies in polysorbate based multi-dose protein formulations: influence on antimicrobial efficacy and potential study approach.
Protein-excipient interactions evaluated via NMR studies in polysorbate based multi-dose protein formulations: influence on antimicrobial efficacy and potential study approach.
Related Articles Protein-excipient interactions evaluated via NMR studies in polysorbate based multi-dose protein formulations: influence on antimicrobial efficacy and potential study approach.
J Pharm Sci. 2018 Jun 05;:
Authors: Torosantucci R, Furtmann B, Elshorst B, Pfeiffer-Marek S, Hartleb T, Andres N, Bussemer T
Abstract
Preservatives are excipients...
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06-10-2018 03:09 AM
Protein-excipient interactions evaluated via NMR studies in polysorbate based multi-dose protein formulations: influence on antimicrobial efficacy and potential study approach
Protein-excipient interactions evaluated via NMR studies in polysorbate based multi-dose protein formulations: influence on antimicrobial efficacy and potential study approach
Publication date: Available online 5 June 2018
Source:Journal of Pharmaceutical Sciences</br>
Author(s): Riccardo Torosantucci, Britta Furtmann, Bettina Elshorst, Stefania Pfeiffer-Marek, Tanja Hartleb, Nikolaus Andres, Till Bussemer</br>
Preservatives are excipients essentially needed in pharmaceutical multi-dose formulations to prevent microbial growth. Among available...
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06-06-2018 01:40 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...
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08-07-2017 07:31 PM
[NMR paper] Electrostatic Energetics of Bacillus subtilis Ribonuclease P Protein by NMR-based Histidine pKa Measurements.
Electrostatic Energetics of Bacillus subtilis Ribonuclease P Protein by NMR-based Histidine pKa Measurements.
Electrostatic Energetics of Bacillus subtilis Ribonuclease P Protein by NMR-based Histidine pKa Measurements.
Biochemistry. 2015 Aug 12;
Authors: Mosley PL, Daniels KG, Oas TG
Abstract
The pKa values of ionizable groups in proteins report the free energy of site-specific proton binding and provide a direct means of studying pH-dependent stability. We measured histidine pKa values (H3, H22, and H105) in the unfolded...
[NMR paper] Tyrosine Phosphorylation within the Intrinsically Disordered Cytosolic Domains of the B-Cell Receptor: An NMR-Based Structural Analysis.
Tyrosine Phosphorylation within the Intrinsically Disordered Cytosolic Domains of the B-Cell Receptor: An NMR-Based Structural Analysis.
Related Articles Tyrosine Phosphorylation within the Intrinsically Disordered Cytosolic Domains of the B-Cell Receptor: An NMR-Based Structural Analysis.
PLoS One. 2014;9(4):e96199
Authors: Rosenlöw J, Isaksson L, Mayzel M, Lengqvist J, Orekhov VY
Abstract
Intrinsically disordered proteins are found extensively in cell signaling pathways where they often are targets of posttranslational...
Influence of an Intrinsically Disordered Region on Protein Domains Revealed by NMR-Based Electrostatic Potential Measurements
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