לוח שנה משולב

The governing role of hydrophobic interactions in countless biological phenomena and technological systems, including protein folding, transmembrane proteins, cell membranes, detergents, paints, decontamination of pollute water, and more, has motivated extensive theoretical and experimental efforts aimed at deciphering the microscopic foundations of this interaction. Yet, after more than a century of extensive research a full predictive theory of this elusive phenomenon is still missing, largely due to the lack of suitable experimental techniques capable of probing the interface between hydrophobic surfaces and water at high enough resolution. In the talk, I will present our recent explorations of this interface using an ultra-high resolution atomic force microscope built in-house for the task and disclose compelling evidence that the hydrophobic interaction reflects a phase transition taking place in the medium when two hydrophobic surfaces approach each other to within a few nanometers. Along the way I'll demonstrate the sub-atomic resolution of our microscope and its value for the study of water structure near surfaces and biomolecules.

Mass spectrometry based proteomics became an enabling technology in the investigation of proteins and proteomes – from protein dynamics, through signaling, protein network interaction to structural determination. The combination of chemical crosslinking of proteins with mass spectrometry (XL-MS) opened up an opportunity to investigate protein-protein interactions within the framework of a whole proteome, even in-vivo, as well as provide a powerful tool for structure determination of proteins and protein complexes. In recent years, improvement in instrumentation and computing power led to improved accessibility of this technique to the non-expert researcher. However, XL-MS suffers from basic deficiencies due to intrinsic issues with sample preparation, data acquisition and analysis. In this tutorial we will discuss current hardware and software capabilities and limitations, and how experiment design can best utilize current capabilities for a successful experiment