Identification of Hydroxyl Protons, Determination of Their Exchange Dynamics, and Characterization of Hydrogen Bonding in a Microcrystallin Protein
Author:
Affiliation:
1. Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Str. 10, D-13125 Berlin, Germany, and Charité Universitätsmedizin, D-10115 Berlin, Germany
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja910167q
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1. Unusual 1H NMR chemical shifts support (His) Cepsilon 1---H{middle dot}{middle dot}{middle dot}O==C H-bond: Proposal for reaction-driven ring flip mechanism in serine protease catalysis
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3. Hydrogen bond dynamics in the active site of photoactive yellow protein
4. Subangstrom Crystallography Reveals that Short Ionic Hydrogen Bonds, and Not a His-Asp Low-Barrier Hydrogen Bond, Stabilize the Transition State in Serine Protease Catalysis
5. Neutron crystallography: opportunities, challenges, and limitations
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