P
Peter J. Knight
Researcher at University of Leeds
Publications - 62
Citations - 5052
Peter J. Knight is an academic researcher from University of Leeds. The author has contributed to research in topics: Myosin & Myosin head. The author has an hindex of 36, co-authored 60 publications receiving 4716 citations. Previous affiliations of Peter J. Knight include University of Bristol.
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Dynein structure and power stroke
TL;DR: In this article, the authors used electron microscopy and image processing to reveal new structural details of dynein c, an isoform from Chlamydomonas reinhardtii flagella, at the start and end of its power stroke.
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Functions and mechanics of dynein motor proteins
TL;DR: A model for the mechanochemical cycle of dynein is emerging, in which nucleotide-driven flexing motions within the AAA+ ring of Dynein alter the affinity of its microtubule-binding stalk and reshape its mechanical element to generate movement.
Journal ArticleDOI
Two-headed binding of a processive myosin to F-actin
Matt L. Walker,Stan A. Burgess,James R. Sellers,Fei Wang,John A. Hammer,John Trinick,Peter J. Knight +6 more
TL;DR: In this paper, the authors used electron microscopy to show that muscle myosin V can span the actin helical repeat (approximately 36 nm) and thus allow single two-headed molecules to transport cargo by walking straight.
Journal Article
The Structural Basis of the Water-Holding, Appearance and Toughness of Meat and Meat Products
Gerald Offer,Peter J. Knight,Robin Jeacocke,Richard Almond,Tony Cousins,John Elsey,Nick Parsons,Alan Sharp,Roger Starr,Peter P. Purslow +9 more
TL;DR: In this article, a structural approach was used to identify which components of the muscle are responsible for its tenderness, water-holding and appearance, and the events that occur during processing.
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Load-dependent mechanism of nonmuscle myosin 2
TL;DR: It is found that human nonmuscle myosins 2A and 2B show marked load-dependent changes in kinetics of ADP release but not in nucleotide binding, which provides a basis for energy-efficient tension maintenance without obstructing cellular contractility driven by other motors such as smooth muscle myosin.