Zhen Wang
Albert Einstein College of Medicine
15 Papers
84 Citations
Zhen Wang is an academic researcher from Albert Einstein College of Medicine. The author has contributed to research in topics: Chemistry & Dihydrofolate reductase. The author has an hindex of 11, co-authored 15 publications. Previous affiliations of Zhen Wang include University of Iowa.
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Papers
Protein Mass-Modulated Effects in the Catalytic Mechanism of Dihydrofolate Reductase: Beyond Promoting Vibrations
TL;DR: Protein mass-modulated vibrations in ecDHFR are involved in TS interactions at cold temperatures and are linked to dynamic motions involved in ligand binding at physiological temperatures, indicating mass effects can affect enzymatic catalysis beyond alterations in promoting vibrations linked to chemistry.
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Human DNMT1 transition state structure.
TL;DR: Understanding the transition state (TS) structure of DNMT1 demonstrates the possibility of using similar analysis to gain subangstrom geometric insight into the complex reactions of epigenetic modifications and demonstrates an approach to understand a complex epigenetic enzyme.
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A remote mutation affects the hydride transfer by disrupting concerted protein motions in thymidylate synthase.
TL;DR: Observations suggest that the Y209W mutation of Escherichia coli TSase disrupts the concerted motions that bring the H-donor and -acceptor together during the pre- and re-organization of the protein environment.
Thymidylate synthase catalyzed H-transfers: two chapters in one tale.
Zhen Wang,Amnon Kohen +1 more
TL;DR: This report compares the physical nature of two sequential H-transfers in the same enzymatic reaction and suggests that TSase optimizes the donor-acceptor geometries for the slower and overall rate-limiting hydride transfer but not for the faster proton transfer.
Hydride Transfer in DHFR by Transition Path Sampling, Kinetic Isotope Effects, and Heavy Enzyme Studies.
TL;DR: This study confirms that fast (femtosecond to picosecond) protein motions in ecDHFR are not coupled to hydride transfer and provides an integrative computational and experimental approach to resolve fast dynamics coupled to chemical steps in enzyme catalysis.