Publications

Thank you for staying tuned!

Tretyachenko V, Vymetal J, Neuwirthova T, Vondrasek J, Fujishima K, Hlouchova K. (2022) Modern and prebiotic amino acids support distinct structural profiles in proteins. Preprint at https://doi.org/10.1101/2021.08.29.458031

Heames B, Buchel F, Aubel M, Tretyachenko V, Lange A, Bornberg- Bauer E, Hlouchova K. (2022) Experimental characterization of de novo proteins and their unevolved random-sequence counterparts. Preprint at https://doi.org/10.1101/2022.01.14.476368

Giacobelli VG, Fujishima K, Lepsik M, Tretyachenko V, Kadava T, Makarov M, Bednarova L, Novak P, Hlouchova K. (2022) In vitro evolution reveals non-cationic protein – RNA interaction mediated by metal ions. Molecular Biology and Evolution, msac032. https://doi.org/10.1093/molbev/msac032.

Fried SD, Fujishima K, Makarov M, Cherepashuk I, Hlouchova K. (2022) Peptides before and during the nucleotide world: and origins story emphasizing cooperation between proteins and nucleic acids. Journal of Royal Society Interface 19: 20210641. https://doi.org/10.1098/rsif.2021.0641

Makarov M, Meng J, Tretyachenko V, Srb P, Březinová A, Giacobelli VG, Bednárová L, Vondrášek J, Dunker AK and Hlouchová K. (2021) Enzyme catalysis prior to aromatic residues: reverse engineering of a dephosphoCoA kinase. Protein Science DOI10.1002/pro.4068

Bornberg-Bauer E, Hlouchova K, Lange A. (2020) Structure and function of naturally evolved de novo proteins. Current Opinions in Structural Biology. 68, 175-183. DOI: 10.1016/j.sbi.2020.11.010

Tretyachenko V, Voráček V, Souček R, FujishimaK, and Hlouchová K. (2020) CoLiDe: Combinatorial Library Design tool for probing protein sequence space. Bioinformatics DOI: 10.1093/bioinformatics/btaa804

Vymětal J, Vondrášek J, and Hlouchová, K. (2019). Sequence Versus Composition: What Prescribes IDP Biophysical Properties? Entropy21(7), 654. https://doi.org/10.3390/e21070654

Tretyachenko V, Vymětal J, Bednárová L, Kopecký V, Hofbauerová K, Jindrová H, Hubálek M, Souček R, Konvalinka J, Vondrášek J, and Hlouchová K. (2017) Random protein sequences can form defined secondary structure and are well-tolerated in vivo. SciRep 7, 15449. https://doi.org/10.1038/s41598-017-15635-8