In research published recently in the online version of the scientific journal Nature Biotechnology, Los Alamos scientists Stéphanie Cabantous, Tom Terwilliger and Geoff Waldo describe a method for engineering soluble, self-associating fragments of green fluorescent proteins that can be used to tag or detect soluble and insoluble proteins in living cells or cell lysates without changing protein solubility.

We all know that it is essential for life. However, probably because of its abundance and simple chemical composition, we often regard this tasteless and odorless substance as being important, but quite simple and ordinary. Scientifically, it is the exact opposite. It appears to show extremely complex and unusual behavior. It is the most studied substance on Earth. Yet, scientists are still puzzled over its strange properties. Even the best computers we have today cannot simulate all of the different properties of water.

Let us look at an example of the surprising properties of water. The strangeness of water starts with the fact that it exists on Earth. Water, being composed of two fairly light atoms (hydrogen and oxygen), should be in the gas phase at the usual temperature ranges that exist in our world. In fact, all compounds that are close to it (i.e. H2S, H2Se, and H2Te) are found mostly in the gas phase. But, compared to similar substances, it melts about 100 degrees above the expected melting point and it boils about 150 degrees above the expected boiling point (see Figure 1). The result is that it is the only material that exists naturally in all three forms (i.e. as ice, liquid, and vapor) on Earth.

In addition to the example given in the previous paragraph, water has at least 40 different surprising properties (See for example the “Forty-one anomalies of water� section in Ref 1). But, what is even more astonishing is the fact that most of these anomalous properties of water are absolutely crucial for life. Simply stated, life on Earth depends on these extraordinary aspects of water. Below we will discuss some of the anomalous properties of water and their importance for life. At the end we will briefly try to explain why water behaves so differently.

Part of a cellular mechanism that regulates the folding of new proteins into their proper shapes also includes a genetic response that enlarges the factory where both protein folding and packaging of proteins occurs. This finding, from researchers at St. Jude Children's Research Hospital, Loyola University (Chicago) and Kyoto University (Kyoto, Japan), are published in the Oct. 15 issue of the Journal of Cell Biology.

The link between protein folding and factory construction ensures that the two processes are coordinated when the cell is called upon to quickly make, fold and secrete large amounts of specific proteins.

The investigators discovered that the cell makes a molecule called XBP1 in response to an increased demand on the protein-folding machinery. This increased demand for folded proteins triggers the so-called unfolded protein response (UPR), as well as the expansion of the factory where proteins are folded and packaged so they can be secreted from the cell. The UPR also prompts the cell to make molecules called chaperones, which do the actual task of protein folding.

XBP1 triggers the cell to make phosphatidylcholine, the major building block of the rows of membranes that make up much of the factory, which is called the endoplasmic reticulum (ER). Membranes in the ER serve as envelopes to package the folded proteins.

A new method to probe the forces that control higher order structure in proteins under native conditions—that is, structure-promoting conditions for the protein—has been developed by chemists at the University of Wisconsin, Madison.

The structure of the chaperonin complex of the bacteria Thermus thermophilus reveals clues about how the important molecule may do its job of folding new or damaged proteins within cells. Led by Professor So Iwata of Imperial College London, the team of scientists announce their findings in this month’s edition of the journal Structure (August 2004).

Although biomimetic nanotechnology is in its infancy, with no applications yet reaching commercialization, the barriers in some cases lie mainly in scaling up production processes to industrial levels. In others, researchers must make significant basic breakthroughs to bridge the gap between laboratory experiments and usefulness.