SOLUTION STRUCTURE OF THE TOXIC E. COLI PEPTIDE, TISB

If you need an accessible version of this item, please submit a remediation request.
Date
2012-04-13
Language
American English
Embargo Lift Date
Department
Committee Members
Degree
Degree Year
Department
Grantor
Journal Title
Journal ISSN
Volume Title
Found At
Office of the Vice Chancellor for Research
Abstract

Antibiotics act by interfering in bacterial metabolism. Thus, antibiotics are only effective against metabolically active bacteria while dormant cells are highly tolerant to antibiotics. Such persistent bacterial cells may be the main culprits in chronic infectious diseases resistance to antimicrobial thera-py. In Escherichia coli, expression of a toxic peptide, TisB, sends cells into dormancy by decreasing the proton motive force thus decreasing ATP levels. TisB is a 29 amino acid residue peptide with 70% hydrophobic residues. It has a predicted alpha helical transmembrane domain spanning residues 6 - 28. In membrane channel studies, ion transport is observed with TisB and with some TisB mutants. As a preliminary to combining multi-dimensional NMR spectroscopy with circular dichroism to determine the structure of the TisB membrane ion transport complex in lipid micelles, NMR spectroscopy is used to determine the structure of TisB in ethanol.

Description
poster abstract
item.page.description.tableofcontents
item.page.relation.haspart
Cite As
Beilin Li, Stephen R. Wassall, Bruce D. Ray, Philip A. Gurnev, and Horia I. Petrache. (2012, April 13). SOLUTION STRUCTURE OF THE TOXIC E. COLI PEPTIDE, TISB. Poster session presented at IUPUI Research Day 2012, Indianapolis, Indiana.
ISSN
Publisher
Series/Report
Sponsorship
Major
Extent
Identifier
Relation
Journal
Source
Alternative Title
Type
Poster
Number
Volume
Conference Dates
Conference Host
Conference Location
Conference Name
Conference Panel
Conference Secretariat Location
Version
Full Text Available at
This item is under embargo {{howLong}}