Atomistic Simulations of the Human Proteasome Inhibited by a Covalent Ligand

Michal H. Kolář (), Lars V. Bock and Helmut Grubmüller
Additional contact information
Michal H. Kolář: Max Planck Institute for Biophysical Chemistry
Lars V. Bock: Max Planck Institute for Biophysical Chemistry
Helmut Grubmüller: Max Planck Institute for Biophysical Chemistry

A chapter in High Performance Computing in Science and Engineering '20, 2021, pp 47-57 from Springer

Abstract: Abstract The proteasome is a large biomolecular complex responsible for protein degradation. It is under intense research due to its fundamental role in cellular homeostasis, and tremendous potential for medicinal applications. Recent data from X-ray crystallography and cryo-electron microscopy have suggested that there is a large-scale structural change upon binding of an inhibitor. We carried out atomistic molecular dynamics simulations of the native and inhibited proteasomes to understand the molecular details of the inhibition. Here we describe the technical details of the simulations and assess the quality of the trajectories obtained. The biochemical aspects of the proteasome are under further investigation and will be published elsewhere. This work was a part of the GSC-Prot project at the HLRS, run on the Cray XC40 supercomputing system.

Date: 2021
References: Add references at CitEc
Citations:

There are no downloads for this item, see the EconPapers FAQ for hints about obtaining it.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:spr:sprchp:978-3-030-80602-6_3

Ordering information: This item can be ordered from
http://www.springer.com/9783030806026

DOI: 10.1007/978-3-030-80602-6_3

Access Statistics for this chapter

More chapters in Springer Books from Springer
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().