J
Jörg Schumacher
Researcher at Technische Universität Ilmenau
Publications - 200
Citations - 4972
Jörg Schumacher is an academic researcher from Technische Universität Ilmenau. The author has contributed to research in topics: Turbulence & Convection. The author has an hindex of 36, co-authored 185 publications receiving 4027 citations. Previous affiliations of Jörg Schumacher include New York University & Yale University.
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Journal ArticleDOI
New perspectives in turbulent Rayleigh-Bénard convection.
Francesca Chillà,Jörg Schumacher +1 more
TL;DR: Key emphasis is given to the physics and structure of the thermal and velocity boundary layers which play a key role for the better understanding of the turbulent transport of heat and momentum in convection at high and very high Rayleigh numbers.
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Turbulent superstructures in Rayleigh-Bénard convection.
TL;DR: Numerical simulations of turbulent convection in fluids at different Prandtl number levels suggest a scale separation and thus the existence of a simplified description of the turbulent superstructures in geo- and astrophysical settings.
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Small-scale universality in fluid turbulence
Jörg Schumacher,Janet D. Scheel,Dmitry Krasnov,Diego Donzis,Victor Yakhot,Katepalli R. Sreenivasan +5 more
TL;DR: The present paper shows that the universal properties of inertial range turbulence (thought to exist only at very high Reynolds numbers) are already present in an incipient way even at modest Reynolds numbers and hence changes the paradigm of research in this field.
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Resolving the fine-scale structure in turbulent Rayleigh–Bénard convection
TL;DR: In this article, high-resolution direct numerical simulation studies of turbulent Rayleigh-Benard convection in a closed cylindrical cell with an aspect ratio of one are presented.
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The ATP hydrolyzing transcription activator phage shock protein F of Escherichia coli: Identifying a surface that binds σ54
Patricia Bordes,Siva R. Wigneshweraraj,Jörg Schumacher,Xiaodong Zhang,Matthew Chaney,Martin Buck +5 more
TL;DR: Nucleotide hydrolysis-dependent presentation of a substrate binding surface can explain why complexes that form between σ54 and PspF are transient and could be part of a mechanism used generally by other AAA+ proteins to regulate activity.