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Yonggun Jun

Researcher at National Central University

Publications -  41
Citations -  1414

Yonggun Jun is an academic researcher from National Central University. The author has contributed to research in topics: Brownian motion & Work (thermodynamics). The author has an hindex of 18, co-authored 38 publications receiving 1155 citations. Previous affiliations of Yonggun Jun include University of California, Irvine & University of Pittsburgh.

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High-Precision Test of Landauer’s Principle in a Feedback Trap

TL;DR: In this article, the authors confirm Landauer's 1961 hypothesis that reducing the number of possible macroscopic states in a system by a factor of 2 requires work of at least kT ln2.
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Invariance of Initiation Mass and Predictability of Cell Size in Escherichia coli

TL;DR: It is shown that cell size in Escherichia coli can be predicted for any steady-state condition by projecting all biosynthesis into three measurable variables representing replication initiation, replication-division cycle, and the global biosynthesis rate, and it is explained why the total cell size is the sum of all unit cells.
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Concentration dependence of the longest relaxation times of dilute and semi-dilute polymer solutions

TL;DR: In this article, the authors studied the longest relaxation times of polymer solutions of semi-flexible T4 DNA and flexible 18 M molar mass polyacrylamide (PAAm) in dilute and semi-dilute concentration range.
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Calibration of Optical Tweezers for In Vivo Force Measurements: How do Different Approaches Compare?

TL;DR: It is discovered that this high-powered trap induces local temperature changes, and an approach to compensate for uncertainties in the magnitude of applied force due to such temperature variations is developed.
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Comprehensive structural model of the mechanochemical cycle of a mitotic motor highlights molecular adaptations in the kinesin family

TL;DR: The contribution of kinesin-5–specific variations to motor function is identified indicating that kinesins indeed are precisely tuned according to cellular function, and multiple adaptations within kinesIn motor domains that tune their mechanochemistries according to distinct functional requirements are highlighted.