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Elan Z. Eisenmesser

Researcher at University of Colorado Denver

Publications -  76
Citations -  4967

Elan Z. Eisenmesser is an academic researcher from University of Colorado Denver. The author has contributed to research in topics: Cyclophilin & Active site. The author has an hindex of 26, co-authored 71 publications receiving 4360 citations. Previous affiliations of Elan Z. Eisenmesser include Purdue University & University of Colorado Hospital.

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Intrinsic dynamics of an enzyme underlies catalysis

TL;DR: It is shown that the intrinsic plasticity of the protein is a key characteristic of catalysis, and the pre-existence of collective dynamics in enzymes before catalysis is a common feature of biocatalysts and that proteins have evolved under synergy pressure between structure and dynamics.
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Enzyme dynamics during catalysis.

TL;DR: The rates of conformational dynamics of the enzyme strongly correlate with the microscopic rates of substrate turnover, which allow a prediction of the reaction trajectory.
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Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair

TL;DR: A comparative and quantitative study of activity, structure and dynamics revealed a close link between protein dynamics and catalytic turnover in hyperthermophilic and mesophilic homologs of adenylate kinase.
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Structural and Biochemical Characterization of the Human Cyclophilin Family of Peptidyl-Prolyl Isomerases

TL;DR: It is found that regions of the isomerase domain outside the proline-binding surface impart isoform specificity for both in vivo substrates and drug design, and it is hypothesized that there is a well-defined molecular surface corresponding to the substrate-binding S2 position that is a site of diversity in the cyclophilin family.
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Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A

TL;DR: CypA does not only bind to CAN but also catalyzes efficiently the cis/trans isomerization of the Gly-89–Pro-90 peptide bond, providing experimental evidence for efficient CypA catalysis on a natively folded and biologically relevant protein substrate.