Matches in SemOpenAlex for { <https://semopenalex.org/work/W2110481446> ?p ?o ?g. }
- W2110481446 endingPage "385" @default.
- W2110481446 startingPage "367" @default.
- W2110481446 abstract "How do molecular motors convert chemical energy to mechanical work? Helicases and nucleic acids offer simple motor systems for extensive biochemical and biophysical analyses. Atomic resolution structures of UvrD-like helicases complexed with DNA in the presence of AMPPNP, ADP.Pi, and Pi reveal several salient points that aid our understanding of mechanochemical coupling. Each ATPase cycle causes two motor domains to rotationally close and open. At a minimum, two motor-track contact points of alternating tight and loose attachment convert domain rotations to unidirectional movement. A motor is poised for action only when fully in contact with its track and, if applicable, working against a load. The orientation of domain rotation relative to the track determines whether the movement is linear, spiral, or circular. Motors powered by ATPases likely deliver each power stroke in two parts, before and after ATP hydrolysis. Implications of these findings for analyzing hexameric helicase, F(1)F(0) ATPase, and kinesin are discussed." @default.
- W2110481446 created "2016-06-24" @default.
- W2110481446 creator A5017311778 @default.
- W2110481446 date "2010-04-01" @default.
- W2110481446 modified "2023-10-18" @default.
- W2110481446 title "Lessons Learned from UvrD Helicase: Mechanism for Directional Movement" @default.
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