Blow, David

Blowing the Theory of How We Smell. David Bradley, Elemental Discoveries, Summer... 

The Flemish painter David Ryckaert s portrait of an alchemist (Figure i6) combines the untidy desk littered with vanitas symbols, the vase (here containing not urine, but the coming-to-form of a homunculus), and the wife. Like Madame de Lavoisier, the wife peers over the shoulder of her seated husband. In Ryckaert s work, the alchemist wears an expression of horror. The glass contains a little man, or perhaps the devil. The wife raises her hand in dismay. Meanwhile, in the corner, a child blows a pig s bladder, a common symbol of futility. 

The importance of oxyanion holes in enzymes was first discovered in chymot-rypsin by David Blow and co-workers and in subtihsin by Jo Kraut and co-workers [39]. In these enzymes, a tetrahedral intermediate is generated after nucleophilic attack of a deprotonated serine side chain on the peptide carbonyl group. It was recognized from the begirming that the geometry of the active site complexes was possibly better complementary to the tetrahedral intermediate than to the planar peptide substrate [40]. 

It is now better known as Molecular Replacement Method. Michael Rossmann and David Blow working in Cambridge, England rediscovered the method... 

The three-dimensional structure of chymotrypsin was solved by David Blow in 1967. Overall, chymotrypsin is roughly spherical and comprises three polypeptide chains, Jinked by disulfide bonds. It is synthesized as a single polypeptide, termed chymotrypainogm, which is activated by the... 

The determination of the three-dimensional structure of chymotrypsin by David Blow in 1967 was a source of further insight into its mechanism of action. Overall, chymotrypsin is roughly spherical and comprises three polypeptide chains, linked by disulfide bonds. It is synthesized as a single polypeptide, termed chymotrypsinogen, which is activated by the proteolytic cleavage of the polypeptide to yield the three chains. The active site of chymotrypsin, marked by serine 195, lies in a cleft on the surface of the enzyme (Figure 9.6). 

One of the most fascinating catalytic systems is the serine 195/histi-dine 57/aspartic acid 102 triad in the proteolytic enzyme chymotrypsin. It was discovered in 1969 by David M. Blow (1931-2004) at Cambridge. The presence of ionic groups in a hydrophobic reaction site enormously increases the basicities and reactivities of these catalytic groups. 

Some meteorites do something amazing—they blow bubbles as they dissolve. David Deamer and Louis Allamandola led a team of researchers who observed this. When they mixed an extract from the meteorite in water, all sorts of carbon-rich oily molecules grouped together, like oil tends to do. These were special, hollow drops called vesicles, like bubbles blown in water with water in the middle. 

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