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Int J Biol Macromol ; 50(1): 1-6, 2012 Jan 01.
Article in English | MEDLINE | ID: mdl-21889533

ABSTRACT

The cAMP receptor protein (CRP) requires cAMP for an allosteric change and regulates more than 150 genes in Escherichia coli. In this study, the modular half of cAMP receptor protein was used to investigate the allosteric signal transmission pathway induced by cAMP binding. The activation of CRP upon cAMP binding is indicated to be realignment of the two subunits within the CRP dimer. The interaction of loop 3 and Phe136 do not involve in signal transmission.


Subject(s)
Cyclic AMP Receptor Protein/chemistry , Escherichia coli/metabolism , Amino Acid Motifs , Calorimetry/methods , Chymotrypsin/chemistry , Circular Dichroism , Cyclic AMP Receptor Protein/metabolism , Dimerization , Escherichia coli Proteins/chemistry , Kinetics , Macromolecular Substances/chemistry , Protein Binding , Protein Conformation , Protein Structure, Tertiary , Signal Transduction , Spectrometry, Fluorescence/methods , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization , Temperature
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