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Michael Härtlein

European Bioinformatics Institute

25

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819

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Investigation into the Relaxation Dynamics of Polymer-Protein Conjugates Reveals Surprising Role of Polymer Solvation on Inherent Protein Flexibility.

2016 Biomacromolecules
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Translational diffusion of hydration water correlates with functional motions in folded and intrinsically disordered proteins

2015 Nature Communications
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Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase.

2014 Acta Crystallographica Section D-biological Crystallography
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Small angle neutron scattering for the study of solubilised membrane proteins.

2013 European Physical Journal E
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A polymer surfactant corona dynamically replaces water in solvent-free protein liquids and ensures macromolecular flexibility and activity.

2012 Journal of the American Chemical Society
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X-ray and neutron small-angle scattering analysis of the complex formed by the met receptor and the Listeria monocytogenes invasion protein InlB

2008 Journal of Molecular Biology
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Coincidence of dynamical transitions in a soluble protein and its hydration water: direct measurements by neutron scattering and MD simulations.

2008 Journal of the American Chemical Society
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Neutrons in biology: Institut Laue – Langevin, 4–7 September 2005

2006 European Biophysics Journal
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A comparison of refined X-ray structures of hydrogenated and perdeuterated rat γE-crystallin in H2O and D2O

2005 Acta Crystallographica Section D-biological Crystallography
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Corrigendum to: Human anti-asparaginyl-tRNA synthetase autoantibodies (anti-KS) increase the affinity of the enzyme for its tRNA substrate 1 (FEBS 24773) 1 Enzyme: asparaginyl-tRNA synthetase (EC 6.1.1.22), EMBL accession number AJ000334.

2001 FEBS Letters
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