title: Chance, destiny, and the inner workings of ClpXP.
abstract: AAA+ proteases are responsible for protein degradation in all branches of life. Using single-molecule and ensemble assays, Cordova et al. investigate how the bacterial protease ClpXP steps through a substrate's polypeptide chain and construct a quantitative kinetic model that recapitulates the interplay between stochastic and deterministic behaviors of ClpXP.
authors.affiliation: Department of Molecular Biosciences and the Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA. Electronic address: rick_russell@cm.utexas.edu.
authors.forename: Rick
authors.initials: R
authors.lastname: Russell
authors.affiliation: Department of Molecular Biosciences and the Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA. Electronic address: matouschek@austin.utexas.edu.
authors.forename: Andreas
authors.initials: A
authors.lastname: Matouschek
mesh_terms: D049071:Endopeptidase Clp / Q000737:chemistry* / Q000378:metabolism*
chemical_list: C568646:ClpP protein, human; D049071:Endopeptidase Clp; C528384:CLPX protein, human
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