Single-molecule mechanobiochemistry

SCIENTIFIC AREA
Protein Structure and Function
CENTER
Centro Nacional de Investigaciones Cardiovasculares "Carlos III" (CNIC)
VACANCIES
1
CONTACT E-MAIL
jalegre@cnic.es
DESCRIPTION OF THE OFFER

Research line: “Characterization of mechanical posttranslational modifications in cardiac proteins”

Summary: The human heart is a formidable mechanical machine that pumps thousands of liters of blood every day. We are far from understanding how the heart works at the molecular level. A key component of heart tissue is the giant protein titin, which sets the passive elasticity of cardiac muscle. Following an interdisciplinary approach that includes proteomics and single-molecule manipulation techniques, we are uncovering posttranslational modifications regulating the elasticity of titin. For more information about the group, please visit: https://www.cnic.es/en/investigacion/single-molecule-mechanobiochemistry

References:

1. Alegre-Cebollada, J., Kosuri, P., Giganti, D., Eckels, E., Rivas-Pardo, J. A., Hamdani, N., Warren, C. M., Solaro, R. J., Linke, W. A. & Fernandez, J. M. S-glutathionylation of cryptic cysteines enhances titin elasticity by blocking protein folding. Cell 156, 1235-1246. (2014).

2. Kosuri, P., Alegre-Cebollada, J., Feng, J., Kaplan, A., Ingles-Prieto, A., Badilla, C. L., Stockwell, B. R., Sanchez-Ruiz, J. M., Holmgren, A. & Fernandez, J. M. Protein folding drives disulfide formation. Cell 151, 794-806. (2012).

MASTER
Biomolecules & Cell D.
Molecular Biomedicine
Biotechnology