Metal-dependent folding of a single zinc finger from transcription factor IIIA. | Zendy

Alan D. Frankel | Zendy; Jeremy M Berg | Zendy; Carl O. Pabo | Zendy

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Metal-dependent folding of a single zinc finger from transcription factor IIIA.

Author(s) -

Alan D. Frankel,

Jeremy M Berg,

Carl O. Pabo

Publication year - 1987

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.84.14.4841

Subject(s) - peptide , zinc finger , circular dichroism , zinc , chemistry , folding (dsp implementation) , peptide sequence , transcription factor , crystallography , biophysics , biochemistry , stereochemistry , biology , gene , organic chemistry , electrical engineering , engineering

A 30-amino acid peptide, which corresponds to the second "zinc finger" domain of transcription factor IIIA, has been synthesized and purified. This peptide folds in the presence of zinc: adding Zn2+ significantly changes the circular dichroism spectrum, and Zn2+ protects the peptide from tryptic digestion. The peptide also binds Co2+, and the absorption spectrum of the Co2+ complex suggests that a tetrahedral binding site is formed by two cysteines and two histidines. Experiments at higher temperatures (60-75 degrees C) suggest that these folded metal-peptide complexes are quite thermostable. The peptide shows some sequence-specific effects in DNase and methylation protection experiments. However, it does not give a clear "footprint," and some effects are observed in the absence of added zinc.

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