A Mechanism to Alter Reversibly the Oligomeric State of a Membrane-bound Protein Demonstrated with Escherichia coliEIImtl in Solution
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
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1. Structural investigation of the transmembrane C domain of the mannitol permease from Escherichia coli using 5-FTrp fluorescence spectroscopy;Biochimica et Biophysica Acta (BBA) - Biomembranes;2012-03
2. Structure of the Cytoplasmic Loop between Putative Helices II and III of the Mannitol Permease of Escherichia coli: A Tryptophan and 5-Fluorotryptophan Spectroscopy Study;Biochemistry;2009-05-14
3. Domain complementation studies reveal residues critical for the activity of the mannitol permease from Escherichia coli;Biochimica et Biophysica Acta (BBA) - Biomembranes;2009-02
4. In vitro Interconversion of the Soluble and Membrane- Integrated Forms of the Escherichia coli Glucose Enzyme II of the Phosphoenolpyruvate-Dependent Sugar-Transporting Phosphotransferase System;Journal of Molecular Microbiology and Biotechnology;2007
5. The oligomeric state and stability of the mannitol transporter, EnzymeIImtl, fromEscherichia coli: A fluorescence correlation spectroscopy study;Protein Science;2006-08
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