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Robert T. Sauer
Researcher at Massachusetts Institute of Technology
Publications - 408
Citations - 42127
Robert T. Sauer is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Repressor & Protein degradation. The author has an hindex of 106, co-authored 402 publications receiving 40181 citations. Previous affiliations of Robert T. Sauer include University of California, San Francisco & Harvard University.
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Flexibility of the yeast alpha 2 repressor enables it to occupy the ends of its operator, leaving the center free.
TL;DR: It is shown that the design of alpha 2 allows a dimer to reach across its operator such that it occupies the two half-sites but leaves the middle of the operator available to other proteins.
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Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine.
Benjamin M. Stinson,Andrew R. Nager,Steven E. Glynn,Karl R. Schmitz,Tania A. Baker,Robert T. Sauer +5 more
TL;DR: It is demonstrated that dynamic interconversion between loadable and unloadable conformations is required to couple ATP hydrolysis by ClpX to mechanical work.
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Mutations in lambda repressor's amino-terminal domain: implications for protein stability and DNA binding
TL;DR: It is argued that mutations that alter solvent-exposed wild-type side chains define residues that form the operator DNA binding surface of lambda repressor whereas completely or partially buried mutations exert their effect by decreasing protein stability.
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Partitioning between unfolding and release of native domains during ClpXP degradation determines substrate selectivity and partial processing
TL;DR: It is shown that model unfolded substrates are engaged rapidly by ClpXP and are then spooled into the degradation chamber at a rate proportional to their length, which prevents trapping of the enzyme in futile degradation attempts and ensures that the energy of ATP hydrolysis is used efficiently for protein degradation.
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NikR Repressor: High-Affinity Nickel Binding to the C-Terminal Domain Regulates Binding to Operator DNA
Peter T. Chivers,Robert T. Sauer +1 more
TL;DR: Nickel binding to a set of low-affinity NikR sites resulted in an additional large increase in operator affinity and substantially increased the size of the NikR footprint on the operator.