Báo cáo khoa học: An Escherichia coli twin-arginine signal peptide switches between helical and unstructured conformations depending on the hydrophobicity of the environment
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The Tat system catalyzes the transport of folded globularproteins across the bacterial plasma membrane and thechloroplast thylakoid. It recognizes cleavable signal peptidescontainingacritical twin-argininemotif but little isknownofthe overall structure of these peptides. In this report, we haveanalyzed the secondary structure of the SufI signal peptide,together with those of two nonfunctional variants in whichthe region around the twin-arginine, RRQFI, is replaced byKKQFI or RRQAA. Circular dichroism studies show thatthe SufI peptide exists as anunstructuredpeptide in aqueoussolvent with essentially no stable secondary structure....
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Báo cáo khoa học: An Escherichia coli twin-arginine signal peptide switches between helical and unstructured conformations depending on the hydrophobicity of the environment
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Báo cáo khoa học: An Escherichia coli twin-arginine signal peptide switches between helical and unstructured conformations depending on the hydrophobicity of the environment
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