Mechanical and functional studies of enzymes at the single molecule level

Mechanical and functional studies of enzymes at the single molecule level

Exhibitor: Christian A.M. Wilson. Profesor asistente, Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile

Date: viernes 28 de octubre 2016, 12:00 – 13:00 hrs. , Café y galletas 11:45 hrs

Place: Auditorio de la Facultad de Ciencias. Av. Gran Bretaña 1111, Playa Ancha, Valparaíso


The effect of force on protein structure an associated changes of protein function is a subject of current intensive research. Mechanical forces are generated inside the cell during such diverse molecular processes as transcription, replication, translation, chromosomal segregation, protein unfolding, translocation of proteins across membranes, cell locomotions among others. Recent technological advances now allow the application and measurement of forces on biomolecules with extreme precision. In particular, the so-called “analytical optical and magnetic tweezers” instruments can manipulate single molecules, such as proteins and nucleic acids, while measuring their internal stress forces generated in the course of biological processes. In this study we used the optical tweezers (OT) to study the mechanical stability of adenylate kinase (AK) from the thermophilic organism Aquifex. AK was first characterized in OT and was found to unfold around 25 pN during force-extension experiments with a fast (mseg) 4 nm intermediate at 15 pN. This intermediate could correspond to the ATP binding domain unfolding independently of the rest of the protein. In another project we study the effect of the chaperon BiP in the folding and unfolding pathways of different protein. We found that BiP bind to the proteins in the unfolded state.
FONDECYT 11130263, PCI PII20150073

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