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The Torque of Rotary F-ATPase Can Unfold Subunit Gamma If Rotor and Stator Are Cross-Linked

During ATP hydrolysis by F(1)-ATPase subunit γ rotates in a hydrophobic bearing, formed by the N-terminal ends of the stator subunits (αβ)(3). If the penultimate residue at the α-helical C-terminal end of subunit γ is artificially cross-linked (via an engineered disulfide bridge) with the bearing, t...

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Autors principals: Hilbers, Florian, Junge, Wolfgang, Sielaff, Hendrik
Format: Artigo
Idioma:Inglês
Publicat: Public Library of Science 2013
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Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC3536650/
https://ncbi.nlm.nih.gov/pubmed/23301103
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pone.0053754
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