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MEMBRANE TRANSPORT STRUCTURE FUNCTION AND BIOGENESIS: Exchangeability of N Termini in the Ligand-gated Porins of Escherichia coli Daniel C. Scott, Zhenghua Cao, Zengbiao Qi, Matthew Bauler, John D. Igo, Salete M. C.
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City

Armstrong / Guterman / San Leandro / Middlesex / Buchanan / Sharma / San Diego / Norman / Nordheim / /

Company

Sigma Chemical Co. / Hercules / Eaton / Ligand / Molecular Biology Inc. / Immusine Corp. / Erithacus Ltd. / Bio-Rad / /

Country

United States / United Kingdom / /

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Facility

N terminus of FhuA / FepA N terminus / FepA vestibule / FhuA C terminus / Medical College of Wisconsin / University of Oklahoma / FepA C terminus / Nucleic Acid Sequence Facility / FhuA N terminus / N terminus / /

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IndustryTerm

biochemical systems / minimal media / cross-linked products / chemical targets / fungal product / metal uptake / energy / metal / detectable cross-linked products / chemical action / energy dependence / 120kDa product / exterior binding site / interior site / /

OperatingSystem

L3 / /

Organization

University of Oklahoma / National Science Foundation / Medical College of Wisconsin / ND ND / Department of Chemistry & Biochemistry / FepA / FhuA and FepA / American Society for Biochemistry / /

Person

John D. Igo / Giovanna Ferro-Luzzi Ames / Emil Gotschlich / Mottur / Zhenghua Cao / Nat / Marjorie Montague / Paul Cook / Physiol / Zengbiao Qi / Ines Chen / Salete M. C. Newton / Richardson / Daniel C. Scott / Charles Earhart / Phillip E. Klebba / Matthew Bauler / Hunt / /

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Position

D. J. / General / cpm/pM / Cao / Major / G. P. / /

Product

Sigma / Franklin / Packard Cobra / /

ProvinceOrState

Wisconsin / New Brunswick / North Dakota / S. K. / Oklahoma / /

PublishedMedium

Molecular Biology / /

Technology

protein engineering / Genetic Engineering / x-ray / electrophoresis / antibodies / directed mutagenesis / spectroscopy / Genotype / gel electrophoresis / /

URL

http /

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