Please use this identifier to cite or link to this item: http://localhost:8081/jspui/handle/123456789/16358
Title: INTERACTION OF CARBON NANOTUBE WITH SELECTED PROTEINS: A MOLECULAR DYNAMICS SIMULATION STUDY
Authors: Saharawat, Rajdeep
Keywords: Higher Temperature;Physiological;Microtubule-Associated Proteins;Intrinsically Disordered Proteins
Issue Date: May-2018
Publisher: I I T ROORKEE
Abstract: The tau proteins were discovered for the first time in 1975 from human brain which associated with the axonal micro-tubular structures1. Tau proteins are stable with respect to the temperature and can exist intact at higher temperature than physiological temperature. They are highly soluble in polar solvents. They belong to a group of protein which is used in the strengthening of microtubules structures and also called as microtubule-associated proteins (MAP) 2. It is observed that tau proteins do not have fixed three-dimensional structure of helix; instead changes continuously and hence belong to Intrinsically Disordered Proteins (IDP). Usually, they found more in upper body parts especially in brain tissues, neurons and in the dendrites. They are abundant in neurons and tissues of the heart, lungs, kidney and skeletal muscles3. Human tau proteins reported in as a composition of 46 amino acids which are placed in a perfect sequence with the help of peptide bond between amino acids and this sequence can be represented as follows4
URI: http://localhost:8081/jspui/handle/123456789/16358
metadata.dc.type: Other
Appears in Collections:MASTERS' THESES (Chemistry)

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