How molecules are linked together to form liquid water is the subject of a groundbreaking study due to appear Thursday, Apr. 1 in Science magazine’s advance publication web site Science Express. The investigation entitled The Structure of the First Coordination Shell in Liquid Water summarizes the results of an international collaboration headed by researchers at Stockholm University and the Stanford Linear Accelerator Center (SLAC) in California. The international team of researchers, which also involved the BESSY synchrotron lab in Berlin, Linköping University and the University of Utrecht, found that water molecules clump together much more loosely than previously thought. The authors propose that this indicates an unknown structure in the liquid, chains or rings or similar – a highly controversial statement which could signify a breakthrough in understanding liquid water.
Water was already in antiquity recognized as one of the fundamental elements in Nature. It is the most abundant substance on earth, and all known forms of life need it to exist. Yet what water really is – at least in its liquid form – is still, to a large extent, a mystery.
Water has a simple chemical formula, H2O, i.e. it consists of two hydrogens and one oxygen. In spite of the apparent simplicity, water is a complex liquid with many unusual properties and many years of intense research have still left much to learn. Even a fundamental question, such as whether or not the liquid has some structure has not been possible to answer directly until now. That is, do the molecules organize themselves in particular ways or is water completely disordered?
Agneta Paulsson | alfa
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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