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Journal Article

IIntron positions in actin genes seem unrelated to the secondary structure of the protein

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Kabsch,  Wolfgang
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Weber, K., & Kabsch, W. (1994). IIntron positions in actin genes seem unrelated to the secondary structure of the protein. EMBO Journal, 13(6), 1280-1286. doi:10.1002/j.1460-2075.1994.tb06380.x.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-A98E-6
Abstract
A catalogue of intron positions along the coding sequence was assembled from the large number of actin genes known for different eukaryotes. 36 positions in the amino acid sequence were compared with the known three-dimensional structure of actin. At least 20 but not more than 23 intron positions are at the start or end of a secondary structural element (beta-strand, alpha-helix or 3/10 helix) while eight positions interrupt such an element. Statistical analysis shows that due to the large number of end positions the boundaries of secondary structural elements are not correlated with the intron positions. In addition, the observed intron pattern seems compatible with the null hypothesis, i.e. intron positions are randomly distributed along the actin sequence.