Metal binding and folding properties of a minimalist Cys2His2 zinc finger peptide

Authors :: Michael, Scott F.
Kilfoil, Valda J.
Schmidt, Michael H
Amann, Barbara T.
Berg, Jeremy M.
Source :: Proceedings of the National Academy of Sciences of the United States. June 1, 1992, Vol. 89 Issue 11, p4796, 5 p.
Publication Year :: 1992
Abstract: A polyanine 26- amino acid peptide characteristic of the TFIIIA-type zinc finger domains has been synthesized and characterized using its metal binding and structural properties. Results show that the peptide folds in the presence of appropriate metal ions to form a complex that has a three-dimensional structure similar to zinc finger domains with more natural sequences. The sequences form a 2:1 peptide/metal complex in which the cysteinate ligands are coordinated to the metal ion but not to histidine.

Subjects :: Peptides -- Synthesis
Protein folding -- Research
Amino acid sequence -- Research
Science and technology

ISSN :: 00278424
Volume :: 89
Issue :: 11
Database :: Gale General OneFile
Journal :: Proceedings of the National Academy of Sciences of the United States
Publication Type :: Academic Journal
Accession number :: edsgcl.13316002

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