M
Michael W. Clarkson
Researcher at Howard Hughes Medical Institute
Publications - 12
Citations - 1054
Michael W. Clarkson is an academic researcher from Howard Hughes Medical Institute. The author has contributed to research in topics: Protein dynamics & Energy landscape. The author has an hindex of 8, co-authored 10 publications receiving 912 citations. Previous affiliations of Michael W. Clarkson include Brandeis University & University of Arizona.
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Journal ArticleDOI
Hidden alternative structures of proline isomerase essential for catalysis
TL;DR: Dual strategies of ambient-temperature X-ray crystallographic data collection and automated electron-density sampling are introduced to structurally unravel interconverting substates of the human proline isomerase, cyclophilin A (CYPA).
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Antiparallel EmrE exports drugs by exchanging between asymmetric structures
Emma A. Morrison,Gregory T. DeKoster,Supratik Dutta,Reza Vafabakhsh,Michael W. Clarkson,Arjun Bahl,Dorothee Kern,Taekjip Ha,Katherine A. Henzler-Wildman +8 more
TL;DR: It is shown that asymmetric antiparallel EmrE exchanges between inward- and outward-facing states that are identical except that they have opposite orientation in the membrane are recorded.
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Transient Non-native Hydrogen Bonds Promote Activation of a Signaling Protein
Alexandra K. Gardino,Janice Villali,Aleksandr Kivenson,Ming Lei,Ce Feng Liu,Phillip Steindel,Elan Z. Eisenmesser,Wladimir Labeikovsky,Magnus Wolf-Watz,Michael W. Clarkson,Dorothee Kern +10 more
TL;DR: The data show that the loss of native stabilizing contacts during activation is compensated by non-native transient atomic interactions during the transition, which unravel atomistic details of native-state protein energy landscapes by expanding the knowledge about ground states to transition landscapes.
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Rescue of conformational dynamics in enzyme catalysis by directed evolution.
Renee Otten,Lin Liu,Lillian R. Kenner,Michael W. Clarkson,Michael W. Clarkson,David Mavor,Dan S. Tawfik,Dorothee Kern,James S. Fraser +8 more
TL;DR: Different biophysical methods are used and mechanistic insights are given into how directed evolution increases the catalytic efficiency of human peptidyl-prolyl cis/trans isomerase CypA, to show how subtle changes can fine-tune enzyme function.
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Free energy landscape of activation in a signalling protein at atomic resolution
Francesco Pontiggia,Dimitar V. Pachov,Michael W. Clarkson,Janice Villali,Michael F. Hagan,Vijay S. Pande,Dorothee Kern +6 more
TL;DR: The free energy landscape of the bacterial response regulator NtrC is explored by combining computation and NMR, and it is found that functional states are defined purely in kinetic and not structural terms.