When a polypeptide binds to DNA, the rotational mobility of a chromophore on the polypeptide is reduced. This simple fact makes it feasible to use polarization of fluorescence methods to study polypeptide-nucleic acid interaction. Previous (l-3) polarization of fluorescence studies of polypeptide-DN
Fractal Geometry Study of DNA Binding Proteins
✍ Scribed by Jun Xu; Yang Chao; Runsheng Chen
- Publisher
- Elsevier Science
- Year
- 1994
- Tongue
- English
- Weight
- 492 KB
- Volume
- 171
- Category
- Article
- ISSN
- 0022-5193
No coin nor oath required. For personal study only.
✦ Synopsis
The main aim of this paper is to search for three-dimensional structure homology between DNAbinding proteins. The run of a protein's main chain is depicted by a sequence, which is constituted by the fractal indices, where each index describes how twisted or extended a partial protein segment is. Two proteins are compared by constructing a dot matrix between two such sequences, and the matrix is searched for dot-concentrated rectangles which is an indication of tertiary homology. This new method is applied to DNA-binding proteins which are selected from Brookhaven Protein Data Bank, among which most contain a helix-turn-helix motif. The dot-matrix shows that there is tertiary homology between two motifs. Other interesting results are also presented in this paper.
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