Sergi Garcia-Mañes (Columbia University, USA)
Dr. Garcia-Mañes will conduct a hands-on experimental approach to
Raul Perez-Jimenez (Columbia University, USA)
demonstrate how protein unfolding is accelerated upon the application of a
constant stretching force. He will also show how the reduction of a single
disulfide bond with simple nucleophiles can be modulated by force. The
experimental demonstration will be complemeted by a discussion on the
molecular determinants that govern protein folding and chemical reactions at
the single molecule level.
Dr. Perez Jimenez will conduct an experimental approach to study
Julio Fernandez (Columbia University, USA)
enzyme catalysis at the single-molecule level using force-clamp technique.
The chemistry of oxidoreductase enzymes will be studied in detail. The latest
research on enzymatic evolution will also be discussed.
Professor Fernandez is the world leader in AFM studies with single
Lorna Dougan (University of Leeds, UK)
proteins. He is the inventor of the so-called Force-clamp technique. In this course,
he will be teaching the capabilities of the force-clamp technique to study both protein
folding and chemical reactions under force.
Dr. Dougan will discuss how single molecule force-clamp spectroscopy
Mariano Carrion-Vazquez (Instituto Cajal, CSIC, Spain)
can be used to explore the role of the solvent environment in protein
folding. This will include methods to determine the importance of
hydrogen bonds in protein structure, the mechanism of osmolyte
stability in protein folding and the specific interactions which
determine extreme mechanical stability in homopolypeptide chains.
Dr. Carrion-Vazquez will focus on the molecular biology of single molecule
Hongbin Li (University of British Columbia, Canada)
experiments. He will explain the importance to construct polyproteins in order to obtain a
reliable, unmistakable fingerprint in single molecule experiments.
Dr. Li will discuss how protein-ligand interactions, including protein-protein
Wolfgang Linke (Ruhr-Universität, Germany)
interaction and protein-metal ion interaction affect the mechanical stability of proteins,
and how such effects can be used to quantitatively determine the binding affinity
of protein-ligand interactions.
Dr. Linke will discuss on the contribution of single molecule AFM to the
Hui Lu (University of Illinois at Chicago, USA)
understanding of the molecular mechanisms determining the elasticity of the giant
protein titin. He will address the latest research regarding how for instance the presence
of disulfide bonds in the N2B sequence of titin control the stiffness of cardiomyocytes.
Dr. Lu will focus on the use of computational methods and theoretical modelling to
study protein mechanics. He will teach steered molecular dynamics (SMD),
which will be used in combination with single-molecule experiments to better understand
protein structure, dynamics and function.