D
Dariush Hinderberger
Researcher at Martin Luther University of Halle-Wittenberg
Publications - 147
Citations - 2847
Dariush Hinderberger is an academic researcher from Martin Luther University of Halle-Wittenberg. The author has contributed to research in topics: Electron paramagnetic resonance & Human serum albumin. The author has an hindex of 28, co-authored 135 publications receiving 2438 citations. Previous affiliations of Dariush Hinderberger include Max Planck Society & ETH Zurich.
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Journal ArticleDOI
Effect of Ionic Liquids on the Solution Structure of Human Serum Albumin
TL;DR: Results indicate that choline dhp as a cosolvent may selectively stabilize HSA conformations closer to the crystal structure out of the overall conformational ensemble.
Journal ArticleDOI
EPR Spectroscopic Characterization of Local Nanoscopic Heterogeneities during the Thermal Collapse of Thermoresponsive Dendronized Polymers
Matthias J. N. Junk,Wen Li,A. Dieter Schlüter,Gerhard Wegner,Hans Wolfgang Spiess,Afang Zhang,Afang Zhang,Dariush Hinderberger +7 more
TL;DR: Despite these efforts, a molecular-scale picture of what happens when thermores-ponsive polymers start to dehydrate at a certain temperature, subsequently collapse, and then assemble to mesoglobules, does not exist.
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Cooperative unfolding of compact conformations of the intrinsically disordered protein osteopontin.
Dennis Kurzbach,Gerald Platzer,Thomas C. Schwarz,Morkos A. Henen,Morkos A. Henen,Robert Konrat,Dariush Hinderberger +6 more
TL;DR: The IDP Osteopontin (OPN), a cytokine involved in metastasis of several types of cancer, is shown to simultaneously sample extended, random coil-like conformations and stable, cooperatively folded conformations.
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EPR spectroscopy reveals nanoinhomogeneities in the structure and reactivity of thermoresponsive hydrogels.
TL;DR: The results show that the system consisting of a statistical binary or tertiary copolymer displays remarkably complex behavior that mimics spatial and chemical inhomogeneities observed in functional biopolymers such as enzymes.
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Evidence for Water-Tuned Structural Differences in Proteins: An Approach Emphasizing Variations in Local Hydrophilicity
TL;DR: Differences in amino acid hydropathies of specific structural regions in both proteins can be used to correlate the observed difference in the global (tertiary) solution structures with the differences on the primary structure level.