Computational design of nanoscale rotational mechanics in de novo protein assemblies. Courbet, A., Hansen, J., Hsia, Y., Bethel, N., Park, Y., Xu, C., Moyer, A., Boyken, S. E., Ueda, G., Nattermann, U., Nagarajan, D., Silva, D., Sheffler, W., Quispe, J., King, N., Bradley, P., Veesler, D., Kollman, J., & Baker, D. Technical Report November, 2021. Company: Cold Spring Harbor Laboratory Distributor: Cold Spring Harbor Laboratory Label: Cold Spring Harbor Laboratory Section: New Results Type: article![Computational design of nanoscale rotational mechanics in de novo protein assemblies [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Natural nanomachines like the F1/F0-ATPase contain protein components that undergo rotation relative to each other. Designing such mechanically constrained nanoscale protein architectures with internal degrees of freedom is an outstanding challenge for computational protein design. Here we explore the de novo construction of protein rotary machinery from designed axle and ring components. Using cryoelectron microscopy, we find that axle-ring systems assemble as designed and populate diverse rotational states depending on symmetry match or mismatch and the designed interface energy landscape. These mechanical systems with internal rotational degrees of freedom are a step towards the systematic design of genetically encodable nanomachines. One-Sentence Summary Computationally designed self-assembling protein rotary machines sample internal degrees of freedom sculpted within the energy landscape.
@techreport{courbet_computational_2021,
title = {Computational design of nanoscale rotational mechanics in de novo protein assemblies},
copyright = {© 2021, Posted by Cold Spring Harbor Laboratory. The copyright holder for this pre-print is the author. All rights reserved. The material may not be redistributed, re-used or adapted without the author's permission.},
url = {https://www.biorxiv.org/content/10.1101/2021.11.11.468255v1},
abstract = {Natural nanomachines like the F1/F0-ATPase contain protein components that undergo rotation relative to each other. Designing such mechanically constrained nanoscale protein architectures with internal degrees of freedom is an outstanding challenge for computational protein design. Here we explore the de novo construction of protein rotary machinery from designed axle and ring components. Using cryoelectron microscopy, we find that axle-ring systems assemble as designed and populate diverse rotational states depending on symmetry match or mismatch and the designed interface energy landscape. These mechanical systems with internal rotational degrees of freedom are a step towards the systematic design of genetically encodable nanomachines.
One-Sentence Summary Computationally designed self-assembling protein rotary machines sample internal degrees of freedom sculpted within the energy landscape.},
language = {en},
urldate = {2022-01-19},
author = {Courbet, A. and Hansen, J. and Hsia, Y. and Bethel, N. and Park, Yj and Xu, C. and Moyer, A. and Boyken, S. E. and Ueda, G. and Nattermann, U. and Nagarajan, D. and Silva, D. and Sheffler, W. and Quispe, J. and King, N. and Bradley, P. and Veesler, D. and Kollman, J. and Baker, D.},
month = nov,
year = {2021},
doi = {10.1101/2021.11.11.468255},
note = {Company: Cold Spring Harbor Laboratory
Distributor: Cold Spring Harbor Laboratory
Label: Cold Spring Harbor Laboratory
Section: New Results
Type: article},
pages = {2021.11.11.468255},
}
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