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Science 26 February 1988:
Vol. 239. no. 4843, pp. 1033 - 1035
DOI: 10.1126/science.3278378
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Articles

Science, Vol 239, Issue 4843, 1033-1035
Copyright © 1988 by American Association for the Advancement of Science

articles

Modulation of folding pathways of exported proteins by the leader sequence

S Park, G Liu, TB Topping, WH Cover, and LL Randall

Biochemistry/Biophysics Program, Washington State University, Pullman 99164.

Leader peptides that function to direct export of proteins through membranes have some common features but exhibit a remarkable sequence diversity. Thus there is some question whether leader peptides exert their function through conventional stereospecific protein-protein interaction. Here it is shown that the leader peptides retarded the folding of precursor maltose-binding protein and ribose-binding protein from Escherichia coli. This kinetic effect may be crucial in allowing precursors to enter the export pathway.


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