Article
ADR1a, a zinc finger peptide, exists in two folded conformations.
Biochemistry - 9 Apr 1991
Xu R X, Horvath S J, Klevit R E
Abstract excerpt
Two-dimensional NMR (2DNMR) studies of several different zinc finger peptides have yielded a picture of the three-dimensional structure of this small DNA-binding motif. Details of the differences among fingers with different sequences may provide some insight into how these domains interact with DNA. Toward this end, we have reanalyzed the 2DNMR spectra of the C-terminal zinc finger sequence from the yeast...
Topics
- Amino Acid Sequence
- DNA-Binding Proteins
- Fungal Proteins
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- Mutation
- Peptide Fragments
- Protein Conformation
- Saccharomyces cerevisiae Proteins
- Transcription Factors
- Zinc Fingers