Title of article
Disruption of coiled coil formation by methionine oxidation
Author/Authors
Carlos Garc?a-Echeverr?a، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 1996
Pages
4
From page
229
To page
232
Abstract
On the basis of previous data, we have designed a leucine-zipper peptide whose folding preferences are controlled by the oxidation state of a single methionine residue. The peptide Ac-Lys-Ala-Glu-Ile-Glu-Ala-Leu-Lys-Ala-Glu-Met-Glu-Ala-Leu-Lys-Ala-Glu-Ile-Glu-Ala-Leu-Lys -Ala-NH2 self-associates in aqueous media to form a parallel coiled coil, but the dimerization function of the peptide is abolished upon conversion of the methionine side chain to its sulfoxide form.
Journal title
Bioorganic & Medicinal Chemistry Letters
Serial Year
1996
Journal title
Bioorganic & Medicinal Chemistry Letters
Record number
787890
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