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@INPROCEEDINGS{Mohanty:1050137,
author = {Mohanty, Sandipan},
title = {{P}rotein {F}olding and {D}esign using {Q}uantum
{A}nnealing},
school = {Forschungszentrum Jülich},
reportid = {FZJ-2025-05841},
year = {2025},
abstract = {Using a simple lattice model with a 2 letter amino acid
alphabet (H: hydrophobic and P: polar), we have explored the
important biophysical problems of protein folding and
protein design. Our formulation of these problems features a
simple algebraic form for the Hamiltonian irrespective of
the system size and composition. Since exact results are
available from for lattice HP chains up to a size of 30, we
were able to thoroughly validate our approach. The D-Wave
advantage quantum annealer successfully identifies the
ground state of the HP model protein chain in $100\%$ of
cases. For a few longer protein chains with up to 64 amino
acids, where exact enumerations were not available but
extensive Monte Carlo studies exist, the D-Wave hybrid
annealer found the correct ground states within minutes,
once again with a $100\%$ success rate. Applying the same
technique to the protein design problem, we found novel HP
protein sequences with the same ground state as the largest
systems we studied for folding. In contrast to the sequences
used for folding, some of our newly found sequences had
unique rather than degenerate ground states.},
month = {May},
date = {2025-05-27},
organization = {IAS Retreat, Jülich (Germany), 27 May
2025 - 27 May 2025},
subtyp = {After Call},
cin = {JSC},
cid = {I:(DE-Juel1)JSC-20090406},
pnm = {5111 - Domain-Specific Simulation $\&$ Data Life Cycle Labs
(SDLs) and Research Groups (POF4-511)},
pid = {G:(DE-HGF)POF4-5111},
typ = {PUB:(DE-HGF)24},
doi = {10.34734/FZJ-2025-05841},
url = {https://juser.fz-juelich.de/record/1050137},
}