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Dutta, Sourav
- Modeling the Interaction of Trehalose-6-Phosphate Synthase and UDP-Glucose Bycomputational Methods
Authors
1 ICAR-Central Island Agricultural Research Institute, Port Blair, Andaman and Nicobar Islands, Pin-744101, IN
2 Techno India University, Biotechnology Dept, EM-4/1, EM Block, Sector V, Salt Lake, Kolkata, West Bengal, Pin-700091, IN
3 Biotechnology Unit, ICAR-Central Research Institute for Jute and Allied Fibres (CRIJAF), Barrackpore, Kolkata -700120, WB, IN
Source
Indian Journal of Bioinformatics and Biotechnology, Vol 3, No 2 (2014), Pagination: 55-69Abstract
Background: Trehalose, an integral component of the cell-wall glycolipids of Mycobacteriumis an unusual nonreducing disaccharide, which plays a variety of biological roles from food storage to cellular protection under diverse environmental stresses (e.g. high pressure, heat-shock, reactive oxygen species, free radicals etc.). Primary enzymatic route to trehalose first involves the transfer of glucose from an UDP-glucose donor to glucose-6-phosphate to form alpha, alpha-1 and 1 trehalose-6-phosphate. It serves as a stress protectant in a range of organisms especially in resurrection of plants and many microorganisms. In addition, the principal role of trehalose is as an important metabolite due to its unique properties like high hydrophobicity, chemical stability, non-hygroscopic glass formation and no internal hydrogen bond formation is worthy to mention.
Methods: MODELLER, a command-line bioinformatics tools and various other bioinformatics programmes and servers like RAMPAGE, PRO-CHECK, Dallite, Errat, Verify 3D were used for analysis and validation of final structures created through homology modeling.
Results: The present work was done for virtual screening of the enzyme Trehalose-6-Phosphate Synthase and studying the interaction with ligand UDP. The crystal structure of TPS-UDP glucose was used for studying the proteinligand interaction. Further homology modeling of the protein was done in detail by deploying basic operation of Argus Lab; Chimer graphics interface to display and manipulate modeled protein.
Application: We report here virtual screening of the enzyme Trehalose-6-Phosphate Synthase to unzip protein-ligand interaction through homology search or comparative modeling to pinpoint potential of the modeled/created protein and to analyze and validate the final structures using various informatics tools.
Keywords
Trehalose-6-Phosphate, UDP-Glucose, Homology modeling, MODELLER, PROCHECK.- Capacity Planning in Client Services and Relationship Management-Maturity Models
Authors
1 Operations Analytics and Consulting Team, FMR, IN
Source
International Journal of Innovative Research and Development, Vol 5, No 9 (2016), Pagination: 59-64Abstract
The Financial Services industry is getting challenged incessantly from fierce competition, rapid change in technology and globalization. Additionally, clients have become more demanding from a service delivery perspective, while continuing to put pressure on cost. All of this is putting significant pressure on margins and the cost of operations. Operational scale and efficiency are of paramount importance today, leading to a focus on building a lean and optimized workforce. To achieve this objective, organizations are increasing focus on Capacity Planning. The traditional methods of demand and capacity planning using volume and time standards work well for contact centers, transaction processing and projects in operations. However, when it comes to the relationships, traditional methods fail as volume and effort here are functions of complexity, subjectivity and quality of relationships.
So, the question arises how do we determine optimal staffing for a relationship management team? This paper proposes methodologies that can help relationship management teams inestimating demand and perform capacity planning, by leveraging analytics. Itlays out a capacity maturity model framework for client services and relationship team. It provides guidance to assess current level and direction to attain next level.