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Ganesan Narsimhan

Researcher at Purdue University

Publications -  141
Citations -  3820

Ganesan Narsimhan is an academic researcher from Purdue University. The author has contributed to research in topics: Adsorption & Emulsion. The author has an hindex of 34, co-authored 140 publications receiving 3465 citations. Previous affiliations of Ganesan Narsimhan include Monash University, Clayton campus & Monash University.

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Rupture of thin stagnant films on a solid surface due to random thermal and mechanical perturbations

TL;DR: The calculated values of rupture time as well as the optimum wavenumber in the present analysis agree well with the results of linear stability analysis for immobile aswell as completely mobile gas-liquid film interfaces.
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Effect of physicochemical properties of peptides from soy protein on their antimicrobial activity.

TL;DR: Though low hydrophobicity and high number of charges help in the formation of water channel for transmembrane aggregates, insertion of peptides with these properties requires overcome of energy barrier, thereby resulting in low antimicrobial activity.
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Pore formation in 1,2-dimyristoyl-sn-glycero-3-phosphocholine/cholesterol mixed bilayers by low concentrations of antimicrobial peptide melittin

TL;DR: A simplified mathematical model for nucleation and growth of pores formed by an aggregate of melittin in lipid bilayer is proposed to predict the variation of rate of dye leakage withMelittin concentration which seems to suggest a toroidal mechanism of pore formation with participation of large number of phospholipid heads.
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Effect of immobilization on the antimicrobial activity of a cysteine-terminated antimicrobial Peptide Cecropin P1 tethered to silica nanoparticle against E. coli O157:H7 EDL933.

TL;DR: Cysteine-terminus modified Cecropin P1 (CP1C, sequence SWLSTAKKLENSAKKRLSEGIAIAIQGGPRC) was chemically immobilized onto silica nanoparticles with maleimide-PEG-NHS ester cross-linkers of different PEG chain lengths to explain the loss of antimicrobial activity of tethered CP1C.
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Characterization of Interfacial Rheology of Protein-Stabilized Air–Liquid Interfaces

TL;DR: In this article, the definition of interfacial dilatational and shear rheology is outlined and the basis of different experimental methods for their characterization is provided, and the connection between interfacial rheological and structure of proteins and other macromolecules is highlighted through the application of polymer theories.