Underlying complexity in the mechanical unfolding of fast folding proteins as explored by atomic force microscopy

  1. Schönfelder, Jörg
Dirigida por:
  1. Raúl Jiménez Pérez Director/a
  2. Víctor Muñoz Director/a

Universidad de defensa: Universidad Autónoma de Madrid

Fecha de defensa: 24 de julio de 2015

Tribunal:
  1. José Manuel Sánchez Ruiz Presidente
  2. Rubén Pérez Pérez Secretario/a
  3. Borja Ibarra Urruela Vocal
  4. Mariano Carrión Vázquez Vocal
  5. Jorge Alegre Cebollada Vocal

Tipo: Tesis

Resumen

Proteins are both flexible polymers and sophisticated nanoscale machines capable of performing a vast display of biological functionalities. All such functions rely on a remarkable trait: the ability of proteins to exploit termal energy to self-assemble (fold) into 3D structures form the chemical blueprints encoded into their amino-acid sequence and change shape in response to stimuli. Deciphering the rules and mecanisms by which proteins fold would have a profound impact in both basic science and biotechnology as it would allow designing proteins with new functionalities a la carte. However, in spite of large scale efforts during the last four decades, we still don't understand how proteins fold nor we are able to design proteins from scratch. (extracto del informe del doctor Don Víctor Muñoz van den Eynde).