North Eastern Hill University

About: North Eastern Hill University is a education organization based out in Shillong, Meghalaya, India. It is known for research contribution in the topics: Population & Ruthenium. The organization has 2318 authors who have published 4476 publications receiving 48894 citations.

Cryopreservation of pharmaceutically important orchid Dendrobium chrysanthum Wall. ex Lindl. using vitrification based method

Abstract: Our present study constitutes the successful and efficient protocol for cryopreservation of Dendrobium chrysanthum. D. chrysanthum Wall. ex Lindl. is a pharmaceutically valuable, ornamental epiphytic orchid of temperate and subtropical regions. On account of excellent herbal medicinal value and horticultural importance, D. chrysanthum is becoming rare due to over exploitation. For long-term conservation of this orchid, protocorm-like bodies of D. chrysanthum were excised and used for cryopreservation by encapsulation–vitrification. In this cryogenic procedure, PLBs were initially osmoprotected with a mixture of 0.4 M sucrose and 2 M glycerol, incorporated in the encapsulation matrix (comprising of 3 % (w/v) sodium alginate and 0.1 M CaCl2). Encapsulated protocorm-like bodies (PLBs) were then precultured on MS liquid medium supplemented with different concentrations of sucrose (0.06, 0.3, 0.5, 0.7 M), and loaded in a loading solution (comprised of 2 M glycerol and 0.4 M sucrose) for different duration to make the precultured PLBs tolerant to plant vitrification solution 2 (PVS2). Subsequently, the PLBs were subjected to PVS2 (Sakai et al. 1990) treatment at different time of exposure (minutes) and temperatures (0 °C and 25 °C). Encapsulated–vitrified PLBs were plunged directly into liquid nitrogen and stored for 1 h. Optimum result (survival 63.2 % and regrowth 59.9 %) was obtained when the beads treated with loading solution for 80 min followed by PVS2 treatment for 100 min. Regenerated plants showed normal morphology as that of control plants.

Periodic Traffic Scheduling for IEEE 802.11ah Networks

Abstract: In this letter, we propose a novel channel access mechanism for IEEE 802.11ah to reduce delay and energy consumption in large-scale networks. The proposed protocol predicts the service interval of a monitoring application and schedules the subsequent frames before their arrivals without requiring any further contention. By doing so, the proposed protocol significantly reduces access delay and unnecessary wake-ups. In saturated network conditions, the proposed protocol shows throughput improvement up to 25%, and reduces average packet latency and energy consumption up to 55.5% and 48.4% respectively as compared to the traditional scheme.

Structural basis of urea-induced unfolding of Fasciola gigantica glutathione S-transferase.

Abstract: Glutathione S-transferases (GSTs) are enzymes that are involved in the detoxification of harmful electrophilic endogenous and exogenous compounds by conjugating with glutathione (GSH) The liver fluke GSTs have multifunctional roles in the host-parasite interaction, such as general detoxification and bile acid sequestration to synthase activity The GSTs have been highlighted as vaccine candidates towards parasitic flukes In this study, we have thoroughly examined the urea-induced unfolding of a mu-class Fasciola gigantica GST1 (FgGST1) using spectroscopic techniques and molecular dynamic simulations FgGST1 is a highly cooperative molecule, because during urea-induced equilibrium unfolding, a concurrent unfolding of the protein without stabilization of any folded intermediate was observed The protein was stabilized with conformational free energy of about ~1236 kcal/mol The protein loses its activity with increasing urea concentration, as the GSH molecule is not able to bind to the protein We also studied the fluorescence quenching of Trp residues and the obtained K SV data that provided additional information on the unfolding of FgGST1 Molecular dynamic trajectories simulated in different urea concentrations and temperatures indicated that urea destabilizes FgGST1 structure by weakening hydrophobic interactions and the hydrogen bond network We observed a precise correlation between the in vitro and in silico studies