Education
- BA, 1972, Biophysics, Amherst College
Research Summary
We study the relationship between protein structure, function, sequence and folding. We focus on the molecular machines that degrade or remodel proteins, targeting proteins for these ATP-dependent reactions. Our experimental tools include biochemistry and single-molecule biophysics, structural biology, protein design and engineering, and molecular genetics.Awards
- Protein Society, Stein and Moore Award, 2013
- Protein Society, Hans Neurath Award, 2007
- Protein Society, Amgen Award, 2001
- National Academy of Sciences, Member, 1996
- American Academy of Arts and Sciences, Fellow, 1993
Key Publications
- Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug. Baytshtok, V, Fei, X, Shih, TT, Grant, RA, Santos, JC, Baker, TA, Sauer, RT. 2021. Cell Rep 34, 108639.
doi: 10.1016/j.celrep.2020.108639PMID:33472065 - Multistep substrate binding and engagement by the AAA+ ClpXP protease. Saunders, RA, Stinson, BM, Baker, TA, Sauer, RT. 2020. Proc Natl Acad Sci U S A 117, 28005-28013.
doi: 10.1073/pnas.2010804117PMID:33106413 - Structural basis of ClpXP recognition and unfolding of ssrA-tagged substrates. Fei, X, Bell, TA, Barkow, SR, Baker, TA, Sauer, RT. 2020. Elife 9, .
doi: 10.7554/eLife.61496PMID:33089779 - Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate. Fei, X, Bell, TA, Jenni, S, Stinson, BM, Baker, TA, Harrison, SC, Sauer, RT. 2020. Elife 9, .
doi: 10.7554/eLife.52774PMID:32108573 - Interactions between a subset of substrate side chains and AAA+ motor pore loops determine grip during protein unfolding. Bell, TA, Baker, TA, Sauer, RT. 2019. Elife 8, .
doi: 10.7554/eLife.46808PMID:31251172