Time filter

Source Type

Rishon LeZion, Israel

The Weizmann Institute of Science is a public research university in Rehovot, Israel. It differs from other Israeli universities in that it offers only graduate and postgraduate tutelage in the science.It is a multidisciplinary research center, with around 2,500 scientists, postdoctoral fellows, Ph.D. and M.Sc. students, and scientific, technical, and administrative staff working at the Institute.Three Nobel laureates and three Turing Award laureates have been associated with the Weizmann Institute of Science. Wikipedia.

Rybtchinski B.,Weizmann Institute of Science
ACS Nano | Year: 2011

Noncovalent systems are adaptive and allow facile processing and recycling. Can they be at the same time robust? How can one rationally design such systems? Can they compete with high-performance covalent materials? The recent literature reveals that noncovalent systems can be robust yet adaptive, self-healing, and recyclable, featuring complex nanoscale structures and unique functions. We review such systems, focusing on the rational design of strong noncovalent interactions, kinetically controlled pathway-dependent processes, complexity, and function. The overview of the recent examples points at the emergent field of noncovalent nanomaterials that can represent a versatile, multifunctional, and environmentally friendly alternative to conventional covalent systems. © 2011 American Chemical Society. Source

Schwarz U.S.,University of Heidelberg | Safran S.A.,Weizmann Institute of Science
Reviews of Modern Physics | Year: 2013

One of the most unique physical features of cell adhesion to external surfaces is the active generation of mechanical force at the cell-material interface. This includes pulling forces generated by contractile polymer bundles and networks, and pushing forces generated by the polymerization of polymer networks. These forces are transmitted to the substrate mainly by focal adhesions, which are large, yet highly dynamic adhesion clusters. Tissue cells use these forces to sense the physical properties of their environment and to communicate with each other. The effect of forces is intricately linked to the material properties of cells and their physical environment. Here a review is given of recent progress in our understanding of the role of forces in cell adhesion from the viewpoint of theoretical soft matter physics and in close relation to the relevant experiments. © 2013 American Physical Society. Source

Gunanathan C.,National Institute of Science Education and Research NISER | Milstein D.,Weizmann Institute of Science
Chemical Reviews | Year: 2014

Activation of inert chemical bonds by transition metal complexes is an area of utmost importance. Efficient bond activation can provide a leading entry to successful catalytic design with the potential of providing greener synthetic methods for useful products. These coordinatively saturated and unsaturated ruthenium pincer complexes with heteroaromatic and aliphatic backbones developed in recent years exhibit new reactivities, activate strong chemical bonds, and act as efficient catalysts for several synthetic methods including unprecedented green transformations, the pivotal interest of this Review. One of the characteristic properties of pincer complexes is the ability to stabilize low valent metal complexes with uncommon geometries. Source

Lev S.,Weizmann Institute of Science
Nature Reviews Molecular Cell Biology | Year: 2010

The movement of lipids within and between intracellular membranes is mediated by different lipid transport mechanisms and is crucial for maintaining the identities of different cellular organelles. Non-vesicular lipid transport has a crucial role in intracellular lipid trafficking and distribution, but its underlying mechanisms remain unclear. Lipid-transfer proteins (LTPs), which regulate diverse lipid-mediated cellular processes and accelerate vectorial transport of lipid monomers between membranes in vitro, could potentially mediate non-vesicular intracellular lipid trafficking. Understanding the mechanisms by which lipids are transported and distributed between cellular membranes, and elucidating the role of LTPs in intracellular lipid transport and homeostasis, are currently subjects of intensive study. © 2010 Macmillan Publishers Limited. All rights reserved. Source

Haran G.,Weizmann Institute of Science
Current Opinion in Structural Biology | Year: 2012

Unfolded proteins under strongly denaturing conditions are highly expanded. However, when the conditions are more close to native, an unfolded protein may collapse to a compact globular structure distinct from the folded state. This transition is akin to the coil-globule transition of homopolymers. Single-molecule FRET experiments have been particularly conducive in revealing the collapsed state under conditions of coexistence with the folded state. The collapse can be even more readily observed in natively unfolded proteins. Time-resolved studies, using FRET and small-angle scattering, have shown that the collapse transition is a very fast event, probably occurring on the submicrosecond time scale. The forces driving collapse are likely to involve both hydrophobic and backbone interactions. The loss of configurational entropy during collapse makes the unfolded state less stable compared to the folded state, thus facilitating folding. © 2011 Elsevier Ltd. Source

Discover hidden collaborations