S
Sathyanarayana N. Gummadi
Researcher at Indian Institute of Technology Madras
Publications - 158
Citations - 2891
Sathyanarayana N. Gummadi is an academic researcher from Indian Institute of Technology Madras. The author has contributed to research in topics: Phospholipid scramblase & Chemistry. The author has an hindex of 25, co-authored 139 publications receiving 2332 citations. Previous affiliations of Sathyanarayana N. Gummadi include Indian Institutes of Technology & University of Wisconsin-Madison.
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Chemical Modification Identifies Two Populations of Glycerophospholipid Flippase in Rat Liver ER
TL;DR: Assays are used to show that proteoliposomes generated from a flippase-enriched Triton X-100 extract of ER can flip analogues of phosphatidylcholine, phosphate-based transport proteins, and that the functionally critical sulfhydryl group in the flipp enzyme protein is buried in a hydrophobic environment in the membrane but becomes reactive on extraction of the protein into Trit on 100.
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Artificial neural network and regression coupled genetic algorithm to optimize parameters for enhanced xylitol production by Debaryomyces nepalensis in bioreactor
TL;DR: In this paper, a multi-layer feed forward neural network (ANN) of 5-10-2 topology has been developed to predict the xylitol production and genetic algorithm (GA) was used to find the optimum parameters to enhance xylanol production.
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What is the role of thermodynamics on protein stability
TL;DR: The authors reviewed various theories that have been proposed to explain the process of protein folding after its biosynthesis in ribosomes and discussed the theories of the determination of the thermodynamic properties and the interpretation of thermodynamic data of protein stability.
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Transbilayer movement of dipalmitoylphosphatidylcholine in proteoliposomes reconstituted from detergent extracts of endoplasmic reticulum. Kinetics of transbilayer transport mediated by a single flippase and identification of protein fractions enriched in flippase activity.
TL;DR: An assay to measure the transbilayer translocation of dipalmitoylphosphatidylcholine, a membrane-embedded phospholipid, in proteoliposomes generated from detergent-solubilized rat liver endoplasmic reticulum is described.
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Microbial pectic transeliminases.
TL;DR: The yields of pectic transeliminases are less than other pectinases, and an improved process for the production of these enzymes is necessary.