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In the present study the price and volume effects changes to the Madrid Stock Exchange fs in Madrid is presented. Bolsa de Madrid (Madrid Stock Exchange) is the largest and most international of Spain's four regional stock exchanges (the others are located in Barcelona, Valencia, and Bilbao) that trade shares and convertible bonds and fixed income securities, also both government and private-sector debt. Bolsa de Madrid is owned by Bolsas y Mercados Espanoles. The researchers have found that the market reacts positively, to news of additions to the index, reflecting pressure on prices of concerned stocks. Trading volumes exhibit commensurate significant changes. While this finding warrants further examination, it leads us to the conclusion that the price effects noted with other index additions may result largely from the demand-supply disequilibrium caused by index, rather than any new information or certification signalled by index inclusion.

The purpose of the present study is to find out the historical volatility of the CNX S&P Nifty and Nikkie225 stock exchanges of India and Japan, respectively. The researchers have also tried to find out the impact of treasury bond rates changes on insurance companies in Japan and banking companies in India. The study done is descriptive in nature where secondary sources were used to collect the data. Purposive sampling technique was used for sampling insurance and banking companies. The sample size was of 8 insurance companies from Nikkie225 and 15 banking companies from NSE CNX S&P Nifty stock exchanges (used in the formulation of index). The study resulted in checking of volatility of Indian Nifty and Japanese Nikkie225 stock exchanges where high-frequency volatility was found out in Nikkie225 exchange. Similarly, it was found that insurance companies of Japan are more volatile to treasury bond rate changes as compared to Indian banking companies.

The glycosylated building block N α-(fluoren-9-ylmethoxycarbonyl)-N γ-[2,3,6-tri-O-acetyl-4-O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-β-D-glucopyranosyl]-L-asparagine pentafluorophenyl ester 7 has been synthesized and incorporated into the solid-phase synthesis of a panel of peptides and N-linked glycopeptides. These have been synthesized as internally quenched fluorogenic compounds where the position of the glycosylated asparagine residue is sequentially varied. Enzymic hydrolysis of these substrates with Savinase has been followed by fluorescence and the kcat/KM-values have been obtained. It is observed that the glycopeptides are less susceptible to proteolytic degradation than are the corresponding peptides.

A panel of α-helical, dimeric coiled-coil peptides has been designed and synthesized for the evaluation of the effect of glycosylation on the conformation of these coiled-coil peptides. Two glycosylated building blocks, Nα -(fluoren-9-ylmethoxycarbonyl)-O-(2,3,4-tri- O-acetyl-6-azido-6-deoxy-β-D -glucopyranosyl)-L-threonine pentafluorophenyl ester 8 and Nα -(fluoren-9-ylmethoxycarbonyl)-O-{2,3,4-tri- O-acetyl-6-[2′-(tert -butoxycarbonylamino)benzoylamino]-6-deoxy-β-D -glucopyranosyl}-L-threonine pentafluorophenyl ester 9 containing the fluorogenic 2-aminobenzamide (Abz) group, have been synthesized. These compounds have been obtained by the glycosylation of Nα-Fmoc-Thr-OPfp with the corresponding glycosyl trichloroacetimidate donors and have been incorporated into the solid-phase synthesis of the peptides 1–3 and 7 and glycopeptides 4–6. Compounds 1 and 4–7 have been synthesized as internally quenched fluorogenic compounds where the Abz group has been employed as the fluorogenic probe and 3-nitrotyrosine Tyr(NO2) as the quenching chromophore. Steady-state fluorescence studies have provided evidence to support the dimerization of the α-helical peptides. Denaturation studies, by fluorescence as well as CD spectroscopy, indicate that the introduction of a carbohydrate moiety into the coiled-coil peptides has a significant destabilizing effect on the α-helicity.