Proteomics

New proteomics study results reported from University of Missouri

Published in Proteomics Weekly, November 2nd, 2009

According to recent research published in the journal Protein Science, "SecB, a remarkable chaperone involved in protein export, binds diverse ligands rapidly with high affinity and low specificity. Site-directed spin labeling and electron paramagnetic resonance spectroscopy were used to investigate the surface of interaction on the export chaperone SecB."

"We examined SecB in complex with the unfolded precursor form of outer membrane protein OmpA as well as with a truncated version of OmpA that includes the transmembrane domain and lacks both the signal peptide and the periplasmic domain. In addition, we studied the binding of SecB to the unfolded mature form of...

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Source: Proteomics Weekly (2009-11-02)

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