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Young C. Kim

Researcher at United States Naval Research Laboratory

Publications -  84
Citations -  3640

Young C. Kim is an academic researcher from United States Naval Research Laboratory. The author has contributed to research in topics: Intrinsically disordered proteins & Macromolecular crowding. The author has an hindex of 27, co-authored 76 publications receiving 2550 citations. Previous affiliations of Young C. Kim include Kyung Hee University & National Institutes of Health.

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Sequence determinants of protein phase behavior from a coarse-grained model.

TL;DR: A novel simulation method to determine thermodynamic phase diagrams as a function of the total protein concentration and temperature is developed and is capable of capturing qualitative changes in the phase diagram due to phosphomimetic mutations of FUS and to the presence or absence of the large folded domain in LAF-1.
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Coarse-grained models for simulations of multiprotein complexes: application to ubiquitin binding.

TL;DR: The coarse-grained models and effective energy functions for simulating thermodynamic and structural properties of multiprotein complexes with relatively low binding affinity and the interactions between ubiquitin and Vps27 are found to be positively cooperative, resulting in a substantial enhancement of the overall binding affinity beyond the approximately 300 microM of the specific domains.
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Relation between single-molecule properties and phase behavior of intrinsically disordered proteins

TL;DR: The results show that these characteristic temperatures are highly correlated, suggesting that experiments performed in dilute conditions may be used to predict phase separation, and suggest that smaller simulations or experiments to determine Tθ or TB can provide useful insights into the corresponding phase behavior.
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SAXS Ensemble Refinement of ESCRT-III CHMP3 Conformational Transitions

TL;DR: An ensemble-refinement method was applied to CHMP3 of ESCRT-III, a protein with multiple helical domains separated by flexible linkers to study dynamic biomolecular assemblies with intrinsically disordered segments.
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TDP-43 α-helical structure tunes liquid–liquid phase separation and function

TL;DR: The TDP-43 helical region serves as a short but uniquely tunable module where application of biophysical principles can precisely control assembly and function in cellular and synthetic biology applications of LLPS.