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Fast NMR-Based Determination of the 3D Structure of the Binding Site of Protein-Ligand Complexes with Weak Affinity Binders.
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- Angewandte Chemie, 2017, v. 129, n. 19, p. 5292, doi. 10.1002/ange.201612304
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Long Distance Measurements up to 160 Å in the GroEL Tetradecamer Using Q-Band DEER EPR Spectroscopy.
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- Angewandte Chemie, 2016, v. 128, n. 51, p. 16137, doi. 10.1002/ange.201609617
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- Article
Fast NMR-Based Determination of the 3D Structure of the Binding Site of Protein-Ligand Complexes with Weak Affinity Binders.
- Published in:
- Angewandte Chemie International Edition, 2017, v. 56, n. 19, p. 5208, doi. 10.1002/anie.201612304
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- Publication type:
- Article
Long Distance Measurements up to 160 Å in the GroEL Tetradecamer Using Q-Band DEER EPR Spectroscopy.
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- Angewandte Chemie International Edition, 2016, v. 55, n. 51, p. 15905, doi. 10.1002/anie.201609617
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- Publication type:
- Article
A weakened interface in the P182L variant of HSP27 associated with severe Charcot‐Marie‐Tooth neuropathy causes aberrant binding to interacting proteins.
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- EMBO Journal, 2021, v. 40, n. 8, p. 1, doi. 10.15252/embj.2019103811
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Defluorination Capability of l‐2‐Haloacid Dehalogenases in the HAD‐Like Hydrolase Superfamily Correlates with Active Site Compactness.
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- ChemBioChem, 2022, v. 23, n. 1, p. 1, doi. 10.1002/cbic.202100414
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- Article
Probing the Interaction of Huntingtin Exon‐1 Polypeptides with the Chaperonin Nanomachine GroEL.
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- ChemBioChem, 2021, v. 22, n. 11, p. 1985, doi. 10.1002/cbic.202100055
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- Article
Rational Structure‐Based Design of Fluorescent Probes for Amyloid Folds.
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- ChemBioChem, 2019, v. 20, n. 9, p. 1161, doi. 10.1002/cbic.201800664
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- Article
Solution NMR Studies of Recombinant Aβ(1-42): From the Presence of a Micellar Entity to Residual β-Sheet Structure in the Soluble Species.
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- ChemBioChem, 2015, v. 16, n. 4, p. 659, doi. 10.1002/cbic.201402595
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Contribution of Specific Residues of the β-Solenoid Fold to HET-s Prion Function, Amyloid Structure and Stability.
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- PLoS Pathogens, 2014, v. 10, n. 6, p. 1, doi. 10.1371/journal.ppat.1004158
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Solid-state NMR sequential assignment of an Amyloid-β(1-42) fibril polymorph.
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- Biomolecular NMR Assignments, 2016, v. 10, n. 2, p. 269, doi. 10.1007/s12104-016-9682-y
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- Article
The NMR² Method to Determine Rapidly the Structure of the Binding Pocket of a Protein--Ligand Complex with High Accuracy.
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- Magnetochemistry, 2018, v. 4, n. 1, p. 1, doi. 10.3390/magnetochemistry4010012
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- Article
Quenched hydrogen-deuterium exchange NMR of a disease-relevant Aβ(1-42) amyloid polymorph.
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- PLoS ONE, 2017, v. 12, n. 3, p. 1, doi. 10.1371/journal.pone.0172862
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