John T. King
University of Michigan
41 Papers
214 Citations
John T. King is an academic researcher from University of Michigan. The author has contributed to research in topics: Chemistry & Spectroscopy. The author has an hindex of 17, co-authored 39 publications. Previous affiliations of John T. King include University of Illinois at Urbana–Champaign.
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Papers
Site-specific coupling of hydration water and protein flexibility studied in solution with ultrafast 2D-IR spectroscopy.
John T. King,Kevin J. Kubarych +1 more
TL;DR: Two-dimensional infrared spectroscopy is used to study the ultrafast hydration and protein dynamics sensed by a metal carbonyl vibrational probe covalently attached to the surface of hen egg white lysozyme dissolved in D(2)O/glycerol solutions.
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Orientation Determination of Interfacial β-Sheet Structures in Situ
TL;DR: The developed method can be used to obtain in situ structural information of beta-sheet components in complex molecules and will greatly broaden the application of optical spectroscopy in physical chemistry, biochemistry, biophysics, and structural biology.
152
Liquid-Liquid Phase Separation of Histone Proteins in Cells: Role in Chromatin Organization
TL;DR: This study demonstrates that the linker histone H1 condenses into liquid-like droplets in the nuclei of HeLa cells and proposes that H1 and DNA act as scaffolds for phase- separated heterochromatin domains.
138
Crowding induced collective hydration of biological macromolecules over extended distances.
TL;DR: Ultrafast two-dimensional infrared (2D-IR) spectroscopy reveals picosecond protein and hydration dynamics of crowded hen egg white lysozyme labeled with a metal-carbonyl vibrational probe covalently attached to a solvent accessible His residue.
137
DNA Local-Flexibility-Dependent Assembly of Phase-Separated Liquid Droplets.
Anisha Shakya,John T. King +1 more
TL;DR: It is found that DNA local flexibility, not simply charge density, determines the LLPS and a role of local DNA flexibility, encoded in the sequence, in the regulation and selectivity of multicomponent LLPS in membraneless intracellular organization is pointed toward.
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