Nov 3 – 4, 2022
Europe/Prague timezone

Conformational behaviour of the uL22 protein

Not scheduled
atrium (IT4Innovations)



Studentská 6231/1B 708 00 Ostrava-Poruba
Poster Poster session Conference Dinner and Poster Session


Petr Linhart


uL22 is one of the universally present ribosomal proteins. Its β-hairpin loop protrudes from the ribosome surface into the exit tunnel. In this work, I have performed all-atom simulations of this isolated uL22 fragment dissolved in water using two different simulation techniques (unbiased molecular dynamics and Hamiltonian Replica Exchange) and 3 force fields. The goal was to examine the behaviour of this fragment, particularly its secondary structure formation tendencies.
I have compared the simulation results with experimental XRD-obtained structure of the fragment when present in the ribosome. I also predicted NMR shifts using the CamShift algorithm and compared them with experimentally measured shifts in order to determine which force field describes the behaviour of the loop most accurately.

Primary author

Petr Linhart

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