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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
Circular permutations of natural protein sequences: structural evidence
1Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden. ylva@alfa.mbb.ki.se
Abstract:
Over the past few years, evidence has accumulated that shows that circularly permuted proteins resulting from permutations in their coding genes can indeed occur naturally. In most instances, these circularly permuted amino acid sequences have been detected by sequence alignment of homologous proteins. Circular permutations may escape detection, however, when based on sequence comparisons alone, as recently illustrated by transaldolase, a member of the class I aldolase family.
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