@article { ISI:000253339800027,
	title = {Sn-119 magic angle spinning NMR of nanocrystalline SnO2},
	journal = {Journal of Nanoscience and Nanotechnology},
	volume = {8},
	number = {1},
	year = {2008},
	month = {JAN},
	pages = {321-328},
	publisher = {AMER SCIENTIFIC PUBLISHERS},
	address = {25650 NORTH LEWIS WAY, STEVENSON RANCH, CA 91381-1439 USA},
	abstract = {<p>Nanocrystalline SnO2 samples of different grain sizes, prepared by inert gas condensation technique (IGCT) and chemical precipitation method and conforming to the tetragonal phase, have been studied by variable speed (3-10 kHz) Sn-119 MAS NMR at 11.74 Tesla field. Sn-119 solid-state NMR results show that the IGCT prepared samples have good crystallinity and phase purity compared to the samples prepared by the chemical method. The determination of Sn-119 chemical shielding parameters (delta(iso), Delta delta and eta) from slow MAS spectra shows that the Sn-119 isotropic chemical shift (delta(iso)) is strongly influenced at smaller grain sizes, attributable to the change in the O2- local symmetry for the surface Sn-119 ions at smaller grain sizes. The observed line widths in MAS spectra are significantly larger than the life-time broadening due to spin-lattice (T-1) and spin-spin (T,) relaxation. The Sn-119 MAS NMR spectra are thus inhomogeneously broadened by a distribution of isotropic chemical shifts, the line broadening increasing with decrease in grain size.</p>},
	keywords = {Hydrolysis, IGCT, MAS NMR, nanocrystalline SnO2},
	issn = {1533-4880},
	doi = {10.1166/jnn.2008.015},
	author = {Sabarinathan, V. and Chandran, C. Vinod and Ramasamy, S. and Ganapathy, Subramanian}
}
@article {45556,
	title = {Structural insights into the unique inhibitory mechanism of Kunitz type trypsin inhibitor from Cicer arietinum L.},
	journal = {Journal of Biomolecular Structure and Dynamics},
	volume = {24},
	year = {2018},
	month = {NOV},
	pages = {1-9},
	type = {Article},
	abstract = {Kunitz-type trypsin inhibitors bind to the active pocket of trypsin causing its inhibition. Plant Kunitz-type inhibitors are thought to be important in defense, especially against insect pests. From sequence analysis of various Kunitz-type inhibitors from plants, we identified CaTI2 from chickpea as a unique variant lacking the functionally important arginine residue corresponding to the soybean trypsin inhibitor (STI) and having a distinct and unique inhibitory loop organization. To further explore the implications of these sequence variations, we obtained the crystal structure of recombinant CaTI2 at 2.8{\r A} resolution. It is evident from the structure that the variations in the inhibitory loop facilitates non-substrate like binding of CaTI2 to trypsin, while the canonical inhibitor STI binds to trypsin in substrate like manner. Our results establish the unique mechanism of trypsin inhibition by CaTI2, which warrant further research into its substrate spectrum. Abbreviations BApNA Nα-Benzoyl-L-arginine 4-nitroanilide BPT bovine pancreatic trypsin CaTI2 Cicer arietinum L trypsin inhibitor 2 DrTI Delonix regia Trypsin inhibitor EcTI Enterolobium contortisiliquum trypsin inhibitor ETI Erythrina caffra trypsin inhibitor KTI Kunitz type inhibitor STI soybean trypsin inhibitor TKI Tamarindus indica Kunitz inhibitor Communicated By Ramaswamy H. Sarma.},
	author = {Bendre, A.D. and Suresh, C.G. and Shanmugam, D. and Ramasamy, S.}
}
@article {44551,
	title = {Structure and function of a highly active Bile Salt Hydrolase (BSH) from Enterococcus faecalis and post-translational processing of BSH enzymes},
	journal = {Biochim Biophys Acta.},
	volume = {1866},
	year = {2018},
	month = {JAN},
	pages = {507-518},
	type = {Journal Article},
	abstract = {Bile Salt Hydrolase (BSH), a member of Cholylglycine hydrolase family, catalyzes the de-conjugation of bile acids and is evolutionarily related to penicillin V acylase (PVA) that hydrolyses a different substrate such as penicillin V. We report the three-dimensional structure of a BSH enzyme from the Gram-positive bacteria Enterococcus faecalis (EfBSH) which has manifold higher hydrolase activity compared to other known BSHs and displays unique allosteric catalytic property. The structural analysis revealed reduced secondary structure content compared to other known BSH structures, particularly devoid of an anti-parallel β-sheet in the assembly loop and part of a β-strand is converted to increase the length of a substrate binding loop 2. The analysis of the substrate binding pocket showed reduced volume owing to altered loop conformations and increased hydrophobicity contributed by a higher ratio of hydrophobic to hydrophilic groups present. The aromatic residues F18, Y20 and F65 participate in substrate binding. Thus, their mutation affects enzyme activity. Docking and Molecular Dynamics simulation studies showed effective polar complementarity present for the three hydroxyl (-OH) groups of GCA substrate in the binding site contributing to higher substrate specificity and efficient catalysis. These are unique features characteristics of this BSH enzyme and thought to contribute to its higher activity and specificity towards bile salts as well as allosteric effects. Further, mechanism of autocatalytic processing of Cholylglycine Hydrolases by the excision of an N-terminal Pre-peptide was examined by inserting different N-terminal pre-peptides in EfBSH sequence. The results suggest that two serine residues next to nucleophile cysteine are essential for autocalytic processing to remove precursor peptide. Since pre-peptide is absent in EfBSH the mutation of these serines is tolerated. This suggests that an evolution-mediated subordination of the pre-peptide excision site resulted in loss of pre-peptide in EfBSH and other related Cholylglycine hydrolases.},
	keywords = {autocatalytic processing, Bile salt hydrolase, molecular dynamics, Mutagenesis, Polar complementarity, X-ray crystallography},
	issn = {15709639},
	doi = {0.1016/j.bbapap.2018.01.003.},
	author = {Chand, D.},
	editor = {Panigrahi, P.}
}
