Laboratorio de Bioquímica

Facultad de Ciencias Químicas y Farmacéuticas

Universidad de Chile

Santos Dumont 964, Independencia

Santiago, Chile 8380494 (Código postal)

Chile Cell-phone: +56-9-9096-9868

Phone: +56-2-29771904


Líneas de Investigación

Our laboratory focuses in single molecule manipulation of biomolecules. This area is a new field of research and allows studying the effect of the forces on the structure of proteins and the concomitant changes in their function. It also permits to determine the forces and torques developed in the course of the mechanochemical conversion in molecular motors. Inside the cell, mechanical forces are produced in molecular processes as diverse as transcription, replication, translation, chromosomal segregation, protein unfolding, translocation of proteins across the membranes and cellular movement. Now, our work is focused in determining the importance of the force associated to the domain movements of BiP (immunoglobulin heavy-chain binding protein)  protein during protein translocation in the ER, also focusing in the kinetic properties of BiP and in the conformational changes that occur during its ATPase cycle, as it is working in the translocation process. However, it’s still not clear the specific mechanism that BiP uses to perfom its work during translocation. This is the reason of the great importance of a detailed study at the single molecule level which will provide information about this important mechanism. One aim is to determine the mechanochemical mechanism that BiP uses working in the translocation. To do this, we are focusing primarily on the study of individual molecules, with optical tweezers, and an innovative combination of magnetic tweezers with TIRF (Total Internal Fluorescence Reflection) using single molecule FRET (Förster Resonance Energy Transfer) dyes.


Publicaciones Recientes

Muñoz, R., Aguilar, F., Wilson, C.A.M., Melo, F. Pulling on super paramagnetic beads with micro cantilevers: single molecule mechanical assay application. Physical Biology.12 (4), 046011, 2015.   

Riedel, C., Gabizon, R., Wilson, C.A.M., Hamadani, K.M., Tsekouras, K., Marqusee, S., Pressé, S., Bustamante, C. The heat released by single catalytic events locally enhances the diffusion of the enzyme. Nature, 517, 227-230, 2015.

Bustamante, C., Kaiser, C.M., Maillard, R.A., Goldman, D., Wilson, C.A.M. Mechanisms of cellular proteostasis: insights from single molecule approaches, Annu. Rev. Biophys. 43, 119-140, 2014.

Preller, A., Wilson, C.A.M, Quiroga, D. Ureta, T. Hexokinase controls the flux through the glycogen synthesis pathway in frog oocytes. FEBS. J. 587, 2825-2831, 2013.

Ramirez-Sarmiento, C.A., Baez, M., Wilson, C.A.M., Babul, J., Komives, E., Guixe, V. Direct observation of solvent penetration during cold denaturation of E. coli phosphofructokinase-2. Biophys. J. 104, 2254-2263, 2013.

Baez, M., Wilson, C.A.M., Ramírez-Sarmiento, C.A., Guixé, V., Babul, J. Expanded Monomeric Intermediate upon Cold and Heat Unfolding of Phosphofructokinase-2 from Escherichia coli. Biophys. J. 103, 2187-2194, 2012.

Baez, M., Wilson, C.A.M., Babul, J. Folding kinetic pathway of phosphofructokinase-2 from Escherichia coli: a homodimeric enzyme with a complex domain organization. FEBS Letters, 585, 2158-2164, 2011.

Rivas-Pardo, J.A., Caniuguir, A., Wilson, C.A.M., Babul. J., Guixe, V. Divalent metal cation requirements of phosphofructokinase-2 from E. coli. Evidence for a high affinity binding site for Mn2+. Archives of Biochemistry and Biophysics, 505, 60-66, 2011.

Wilson, C.A.M.  Preller, A., Valenzuela, M.A., Ureta, T. Measurement of Glycogen Synthase Activity in Crude Extracts by CE. Electrophoresis (Wiley), 28, 2888-2892, 2007.

 Otras Publicaciones

Single Molecule Studies by Optical Tweezers: Folding and Unfolding of Glucokinase from Thermococcus litoralis. Wilson, C.A.M. Tesis para obtener el grado de Doctor, Facultad de Ciencias, Universidad de Chile, 2011.

Caudiverbera caudiverbera (Linneaus) oocytes: Control coefficients for UDP-glucose pyrophosphorylase and glycogen synthase in glycogen synthesis pathway. Wilson, C.A.M. Tesis para obtener el grado de Bioquímicos, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, 2008.

El cincuentenario de la carrera bioquímica en la Universidad de Chile: antecedentes y reflexiones sobre el antes y el después (50th anniversary of Biochemistry school in Universidad de Chile: antecedents and reflections about before and after). Sapag Hagar, M., Cotoras, D., Israel, Y., Pizarro, J., Puente, J., Rojas, C., Romero, C., Rosemblatt, M., Wilson, C. Facultad de Ciencias Químicas y Farmacéuticas. Universidad de Chile. 2007.




Wilson, C.A.M., Contreras, G.I., and Babul, J. Solicitante: Universidad de Chile (2014) Método de visualización de biomoléculas a simple vista, tales como proteínas o ácidos nucleicos, sin la necesidad de usar compuestos potencialmente tóxicos, exposición a la luz ultravioleta (UV) o fluorescencia. Número de solicitud en Chile (INAPI) 3000-2014. Solicitada.