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dc.contributor.authorLove, Chloe R.
dc.description1 Broadside. 48"W x 36"Hen_US
dc.description.abstractThe bacterial flagellum is a highly conserved, autoassembling structure which enables motility. The flagellum consists of three parts: a basal body inside the cell, a hook structure, and an external flagellar filament, which is typically several times longer than the cell body. The flagellar filament is a narrow tube-like structure composed of a single protein, flagellin, which is diffused down the channel at the center of the filament as it is assembled. Four amino acids constitute the flagellar channel. The terminal amino acid which lines this channel is arginine, which is polar and carries a positive charge. This study endeavored to ascertain whether the positive charge, polarity, or size of arginine is necessary for protein transport and successful auto-assembly of the flagellar filament.en_US
dc.description.sponsorshipKalamazoo College. Department of Biology. Diebold Symposium, 2019en_US
dc.publisherKalamazoo, Mich. : Kalamazoo Collegeen_US
dc.relation.ispartofKalamazoo College Diebold Symposium Presentation Collectionen
dc.rightsU.S. copyright laws protect this material. Commercial use or distribution of this material is not permitted without prior written permission of the copyright holder.en
dc.titleEffect of site-directed replacement mutations to channel-lining arginine in flagellin on protein transport and motility in Salmonella typhimuriumen_US

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  • Diebold Symposium Posters and Schedules [479]
    Poster and oral presentations by senior biology majors that include the results of their Senior Integrated Projects (SIPs) at the Diebold Symposium. Abstracts are generally available to the public, but PDF files are available only to current Kalamazoo College students, faculty, and staff.

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