Proteins in figurative arts and artworks
ESR1: Proteins in figurative arts and artworks (@ UoL).
Objectives: (i) identification of proteins in paint binders and their biological origins for a better understanding of artworks, (ii) identification of protein chemical modifications (due to local environment, pollution, restoration treatments, conservation conditions, etc.) for a better knowledge of artwork conservation/degradation.
Expected Results: The impact of commonly used restoration tools will be defined at molecular level. Proteins truncations and chemical modifications will be determined. Identification of common and uncommon protein modifications, identification of biological species, study of proteins from unsequenced genomes will be massively improved.
The analysis of proteins in figurative arts includes (i) the identification of proteins and their biological origins for a better understanding of artworks, (ii) but also the identification of protein chemical modifications (due to local environment, pollution, restoration treatments, conservation conditions, etc.) for a better knowledge of artwork conservation/degradation. ESR1’s activity will be divided in technical sessions (bottom up and top down experiments), visit of museums and their restoration/conservation sections and study of specific artworks. The interactions with museums, conservators and restorers will be done via (i) the LeadART network (resulting from JPI-JHEP project 2014-2017, coordinator: C. Tokarski), and (ii) the NordART network (coordinator C. Tokarski) that links research, museums (Louvre, Matisse museum, etc.) and archaeology in the North of France. The analytical sessions will include both bottom up and top down approaches. Bottom-up proteomics is the current proteomics mainstream. Particular focus will be given to sample preparation (according to the type of sample), analytical workflow adapted to the study of very small sample amounts (on-line nanoLC nanoESI-Orbitrap MS), instrument settings, and bioinformatic tools (commercial softwares and custom-developed ones) used for protein identification, identification of common and uncommon protein modifications, identification of biological species, study of proteins from unsequenced genomes. The second part of the analytical session will focus on the top down approach (see Chem Rev 2015), using a high-resolution MS analyzer and the direct fragmentation of proteins without preliminary chemical or enzymatic hydrolysis. Particular cautions related to the sample preparation are needed and will be shown during ESR1’s project (e.g. intact proteins extraction from their complex matrix). Top down experiments will be applied to the study of protein extracts from various ancient artworks using nanoLC nanoESI-Qh-FT-ICR MS including CID (Collision Induced Dissociation), ECD (Electron Capture Dissociation) and IRMPD (InfraRed MultiPhoton Dissociation) experiments. The impact of commonly used restoration tools will be studied at molecular level on model samples formulated in the lab with ancient recipes and on ancient samples restored/non restored in Partners’museums. Proteins truncations and chemical modifications will be studied.
Networking. Within TEMPERA, ESR1 will interact more closely with:
- ESR2: ESR1 will spend a secondment period of 4 months in UCPH (co-supervision) to share and compare experience in paint binders analysis.
- ESR1 will spend a secondment period, 3 months, at the conservation section of one of the Museum in the NordART network, to optimise, together with curators and restorers, the most effective and less invasive sampling procedure.
- ESR1 will share samples with UCAS, to contrast with pigment investigations on materials in China and ESR2
Planned secondment(s): 4 months at UCPH to share and compare experience in paint binders analysis, 3 months, at one of the Museum in the NordART network.
DISCLAIMER: The information reported on this website reflects only the TEMPERA consortium view. The European Research Agency is not responsible for any use that may be made of the information it contains.
🇪🇺 This project has received funding from the European Union's EU Framework Programme for Research and Innovation Horizon 2020 under Grant Agreement No. 722606. 🇪🇺