There is, I think, something ethereal about i —the square root of minus one. I remember first hearing about it at school. It seemed an odd beast at that time—an intruder hovering on the edge of reality.

Usually familiarity dulls this sense of the bizarre, but in the case of i it was the reverse: over the years the sense of its surreal nature intensified. It seemed that it was impossible to write mathematics that described the real world in …

I and i

Data Mining Practical Machine Learning Tools and Techniques

J. Appl. Cryst.の発刊に際して

I read this book the same weekend that the Packers took on the Rams, and the experience of the latter event, obviously, colored my judgment. Although I abhor anything that smacks of being a handbook (like, \"How to Earn a Merit Badge in Neurosurgery\") because too many volumes in biomedical science already evince a boyscout-like approach, I must confess that parts of this volume are fast, scholarly, and significant, with certain reservations. I like parts of this well-illustrated book because Dr. Sj6strand, without so stating, develops certain subjects on technique in relation to the acquisition of judgment and sophistication. And this is important! So, given that the author (like all of us) is somewhat deficient in some areas, and biased in others, the book is still valuable if the uninitiated reader swallows it in a general fashion, realizing full well that what will be required from the reader is a modulation to fit his vision, propreception, adaptation and response, and the kind of problem he is undertaking. A major deficiency of this book is revealed by comparison of its use of physics and of chemistry to provide understanding and background for the application of high resolution electron microscopy to problems in biology. Since the volume is keyed to high resolution electron microscopy, which is a sophisticated form of structural analysis, but really morphology in a modern guise, the physical and mechanical background of The instrument and its ancillary tools are simply and well presented. The potential use of chemical or cytochemical information as it relates to biological fine structure , however, is quite deficient. I wonder when even sophisticated morphol-ogists will consider fixation a reaction and not a technique; only then will the fundamentals become self-evident and predictable and this sine qua flon will become less mystical. Staining reactions (the most inadequate chapter) ought to be something more than a technique to selectively enhance contrast of morphological elements; it ought to give the structural addresses of some of the chemical residents of cell components. Is it pertinent that auto-radiography gets singled out for more complete coverage than other significant aspects of cytochemistry by a high resolution microscopist, when it has a built-in minimal error of 1,000 A in standard practice? I don't mean to blind-side (in strict football terminology) Dr. Sj6strand's efforts for what is \"routinely used in our laboratory\"; what is done is usually well done. It's just that …

Methods in Enzymology.

Structure and nanostructure in ionic liquids.

Fuculose phosphate aldolase catalyzes the reversible cleavage of fuculose-1-phosphate to dihydroxyacetone phosphate and l-lactaldehyde. A tetramer by nature, this enzyme from Thermus thermophilus HB8 represents the group of Class II aldolases. The structure was solved in two different space groups using the crystals obtained from slow evaporation vapour-diffusion and microbatch techniques. The detailed crystallization description has been reported previously. In this study, the structural features of fuculose phosphate aldolase from T. thermophilus have been explored extensively through sequence and structure comparisons with fuculose phosphate aldolases of different species. Finally, an in silico analysis using induced fit docking was attempted to deduce the binding mode of fuculose phosphate aldolase with its natural substrate fuculose-1-phosphate along with a substrate analog dihydroxyacetone phosphate and phosphoglycolohydroxymate—a potential aldolase inhibitor. The results show the mechanism of action may be similar to that of Escherichia coli fuculose aldolase.

Crystal structure analysis of l -fuculose-1-phosphate aldolase from Thermus thermophilus HB8 and its catalytic action: as explained through in silico

In the title compound, C19H21BrN2O2S, the fused pyrrolidine rings adopt envelope conformations. The mol­ecular packing is stabilized by weak inter­molecular C—H⋯O inter­actions and van der Waals forces.

1‐(p‐Bromo­phen­yl)‐5‐p‐tosyl­perhydro­pyrrolo[3,4‐b]pyrrole

Fumarase catalyzes the reversible, stereospecific hydration/dehydration of fumarate to L-malate during the Kreb’s cycle. In the crystal structure of the tetrameric fumarase, it was found that some of the active site residues S145, T147, N188 G364 and H235 had water-mediated hydrogen bonding interactions with pyromellitic acid and citrate which help to the protonation state for the conversion of fumarate to malate. When His 235 is mutated with Asn (H235N), water-mediated interactions were lost due to the shifting of active site water molecule by 0.7 A away. Molecular dynamics (MD) simulations were also carried out by NAMD and analyzed using Assisted Model Building with Energy Refinement (AMBER) program to better understand the conformational stability and other aspects during the binding of pyromellitic acid and citrate with native and mutant FH. The role of hydrogen bonds and hydrophobic interactions was also analyzed. The present study confirms that the H235N mutation has a major effect on the catalytic ...

Molecular docking and molecular dynamics simulations of fumarate hydratase and its mutant H235N complexed with pyromellitic acid and citrate

1-{2-[(4-Nitrobenzylidene)amino]phenyl}-3-phenylthiourea

In the title mol­ecule, C19H15N7, the dihedral angle between the two benzotriazole moieties is 7249 (6)° and those between the pyridine and the two benzotriazole moieties are 7026 (6) and 5770 (7)° The crystal structure is stabilized by intermolecular C—H⋯N and C—H⋯π interactions

Devadasan Velmurugan

Papers

Crystal structure analysis of l -fuculose-1-phosphate aldolase from Thermus thermophilus HB8 and its catalytic action: as explained through in silico

1‐(p‐Bromophenyl)‐5‐p‐tosylperhydropyrrolo[3,4‐b]pyrrole

Molecular docking and molecular dynamics simulations of fumarate hydratase and its mutant H235N complexed with pyromellitic acid and citrate

1-{2-[(4-Nitrobenzylidene)amino]phenyl}-3-phenylthiourea

2,6-Bis(N,N′-benzotriazol-1-ylmethyl)pyridine

Devadasan Velmurugan

Papers

Crystal structure analysis of l -fuculose-1-phosphate aldolase from Thermus thermophilus HB8 and its catalytic action: as explained through in silico

1‐(p‐Bromo­phen­yl)‐5‐p‐tosyl­perhydro­pyrrolo[3,4‐b]pyrrole

Molecular docking and molecular dynamics simulations of fumarate hydratase and its mutant H235N complexed with pyromellitic acid and citrate

1-{2-[(4-Nitrobenzylidene)amino]phenyl}-3-phenylthiourea

2,6-Bis(N,N′-benzotriazol-1-ylmethyl)pyridine

1‐(p‐Bromophenyl)‐5‐p‐tosylperhydropyrrolo[3,4‐b]pyrrole