Mikhail Makarov

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.

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.