Klára Hlouchová

This study compares how different cationic chemistries influence peptide-RNA coacervation, showing that statistical peptide ensembles can drive protoribosomal condensate formation without sequence-specific optimization.

This paper introduces a high-throughput method for screening protein solubility using aqueous solvents, demonstrating its effectiveness with challenging de novo proteins.

The paper explores random protein sequence space to identify physical phenotypes and shows that sequence-based models can predict experimentally observed properties.

The paper shows that peptides made from non-standard amino acids can form protein-like secondary structures, expanding the known sequence-structure space beyond Earth's 20 amino acids.

This study examines protein-coenzyme interactions in the Protein Data Bank to assess the plausibility of early peptide-cofactor collaborations before the Central Dogma.

This study shows random 25-mer peptides with a prebiotically plausible amino acid alphabet can self-assemble into thermostable beta-rich nanostructures.

The paper designs ancient proteins using a limited amino acid set and shows they are stable and mutation-resilient.

This study investigates how peptides interact with mineral surfaces and lipid vesicles, showing acidic residues bind minerals and arginine enhances phosphate mobilization, while different amino acid alphabets affect vesicle stability.

This paper investigates the role of ribosomal peptides in protoribosome compartmentalization and stability, showing that RNA-protein interactions protect RNA from degradation and influence structural flexibility.

This study identifies human de novo proteins with high folding potential by screening for structural compactness and disorder using FRET and FACS.

This study shows that proteins made from prebiotic and modern amino acids can form stable structures, challenging the idea that complex amino acids are necessary for protein folding.