Conformation-Dependent Hydrogen-Bonding Interactions in a Switchable Artificial Metalloprotein.
Sign Up to like & getrecommendations! Published in 2024 at "Biochemistry"
DOI: 10.1021/acs.biochem.4c00209
Abstract: Hydrogen-bonding (H-bonding) interactions in metalloprotein active sites can critically regulate enzyme function. Changes in the protein structure triggered by interplay with substrates, products, and partner proteins are often translated to the metallocofactor by way of… read more here.
Keywords: conformation; bonding interactions; hydrogen bonding; switchable artificial ... See more keywords
Engineering a Conformationally Switchable Artificial Metalloprotein.
Sign Up to like & getrecommendations! Published in 2022 at "Journal of the American Chemical Society"
DOI: 10.1021/jacs.2c08885
Abstract: Many naturally occurring metalloenzymes are gated by rate-limiting conformational changes, and there exists a critical interplay between macroscopic structural rearrangements of the protein and subatomic changes affecting the electronic structure of embedded metallocofactors. Despite this… read more here.
Keywords: artificial metalloprotein; engineering conformationally; switchable artificial; conformationally switchable ... See more keywords