Computational Approaches in Chlamydomonas reinhardtii for by Pratyoosh Shukla, M.V.K. Karthik

By Pratyoosh Shukla, M.V.K. Karthik

This e-book describes the feasibility of utilizing molecular dynamics as a screening strategy to determine the soundness of HydA1 and PetF interactions. Structure-based computational techniques are essential to realize and signify protein-protein complexes and their features. It introduces the concept that for particular proteins, homology modeling is the simplest method and that docking algorithms are an more and more strong device for delivering an in depth rationalization of such interactions. This e-book is an invaluable resource of knowledge on biomass-based biofuels for researchers within the box of bio-hydrogen and bioinformatics thoughts. Biofuel and bioenergy made from unicellular microalgae Chlamydomonas reinhardtii is a fresh power resource and supplying information regarding sensible optimization in HydA1 and PetF interactions might help researchers to undertake fast screening how to determine key protein complexes and their capabilities. The publication additionally offers an creation to hydrogenases and linked Chlamydomonas reinhardtii, that is an invaluable version microorganism for study on biofuel creation. The booklet specializes in the in silico equipment corresponding to phylogenetic stories, homology modeling, molecular docking, electrostatic experiences and conformational research, that have the aptitude to turn into the main reasonably priced equipment for bio-fuel production.

This publication offers a helpful source to senior undergraduate and graduate scholars, researchers, execs and different members or teams operating within the quarter of bioenergy with specific connection with microalgal biofuel.

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Extra info for Computational Approaches in Chlamydomonas reinhardtii for Effectual Bio-hydrogen Production

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Interaction studies in the present work reported that hydA1 had better interaction with petF as compared to hydA2 and phylogenetic analysis depicted that Arg84, Lys85, Gly104, Gly108, Ser230 and Asp249 as conserved binding site residues. Moreover during the present study it was stated that amino acids viz. Leu119, Glu141 and Gly142 are responsible for conformational change of HydA1 model. This happens due to their interaction with petf where they change from coil to extended conformations resulting stability in hydA1-petF complex.

Nature 438(7067):449–453 Eswar N, Marti-Renom MA, Webb B, Madhusudhan MS, Eramian D, Shen M, Pieper U, Sali A (2006) Comparative protein structure modeling with MODELLER. 30, Wiley Fiser A, Do RK, Sali A (2000) Modeling of loops in protein structures. Protein Sci 9:1753–1773 Fontecilla-Camps JC et al (2007) Structure/function relationships of [NiFe]- and [FeFe]hydrogenases. Chem Rev 107(10):4273–4303 Fukuzawa H, Miura K, Ishizaki K, Kucho KI, Saito T, Kohinata T, Ohyama K (2001) Ccm1, a regulatory gene controlling the induction of a carbon-concentrating mechanism in Chlamydomonas reinhardtii by sensing CO2 availability.

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