PeptideBooogie is an artistic research about protein structures.
My original idea was to convert protein structures into chamber music.

Proteins are large biomolecules, consisting of one or more long chains of amino acid residues. There is a basic “alphabet” of 20 different amino acids:
molecular_structures_of_the_21_proteinogenic_amino_acidsProteins perform a vast array of functions within organism, including catalysing metabolic reaction, DNA replication, responding to stimuli and transporting other molecules. They differ from one another primarily in their sequence of amino acids, which usually results in protein folding into a specific 3D structure that determines its activity.
The polypeptide chain (the chain of amino acids) folds itself in the space like a ribbon, making two different twists in proximity of every single amino acid (dihedral angles φ (phi) and ψ (psi)).
dihedralI looked for a music (a melody) following the protein backbone, as it were traveling along the peptide ribbon, twisting in melodic intervals as the ribbon twists in 3D space.
The narrower the angle, the wider the musical interval; for instance, zero degrees = unison, 60 degrees = major third…
Then I created a software (using Processing language) that takes the PDB detailed description of a protein (from the RCSB online database), computes the dihedral angles (not provided in the numerical model) and finally transforms the sequence in a melody (a midi file). Additionally, different amino acids produces different couples of notes, on a rythmical point of view. Amino acids with little molecular weight produces faster notes, and some features like sulphur atoms or aromatic rings produce other rythmical patterns.
scheme-pdb2midAfter this transformation from the “molecular domain” to the “musical domain”, what arises is that some specific features are preserved and recognizable.
For instance, a “zig-zag folding” of the polypeptide creates a so-called beta-sheet, like a wider molecular piece of ribbon. A helicoidal folding  creates conversely a so-called alpha-helix, like molecular curls.
protein_foldingThe musical equivalents are “zig-zag” patterns for beta-sheets, generating a wandering, steady melody:
music-betaand a “curling” pattern for alpha-helix, a constant upward musical movement, spanning chromatic or diatonic scales, which has been constrained to 2 octaves (just to make it less extreme to perform):
music-alphaHence, alternating angles produce musical intervals going up and down around a center, but a sequence of angles (all positive or all negatives) produce something like a “musical scale”.

Upon this computer generated “molecular music”, intended to be played by a flute, I wrote the piano score, giving some harmonic flavor and making the result a little more human to listen. The proteins I chose are important to humans and life in general, hence I wanted a “human music”, played live by performers, not some electronic or recorded music, but old-fashion chamber music, thriving of “hic et nunc”.
1OVA is the ovoalbumin, an amazing energy source contained in egg white and one of the first proteins to be studied. 3RGK is the myoglobin, an iron-and oxygen- binding protein found in the muscle tissue. 4K3S is a “DNA sliding clamp”… sort of ring which slides along genetic code, involved in its reduplication process.
The weird melodies generated from the protein structure werw performed live by a piano player (Sonia Cugini) and a flute player (Alberto Piovesan).
img_0280 schermata-2016-01-20-alle-11-11-3812032215_10206672007991367_3176562062603198355_nThe music performance was accompanied by a video projection of Cecilia Donaggio and a the movements of the performer Betta Porro (alias “Lady Protein”). We performed in 2015 at


In 2016-2017 a video was present at the exhibition “Arte-Scienza-Biotecnologia” – Museo Nacional de la Màscara – San Luis Potosì (Mexico).

The project was initially ideated for the exhibition “Arte/Scienza/Biotecnologia”, by Gruppo78 Contemporary Art.

All the work of research was made in collaboration with Silvia Onesti, head of the Structural Biology Lab at Sincrotrone – Trieste.