A linearized notation for the secondary structure of proteins, involving a three-dimensional → one-dimensional transformation, has been devised on the basis of peptide conformational energy hypersurface topology. Such a linearized notation of protein secondary structures can provide a description of the three-dimensional structure without relying on the concept of "unordered" conformational states. On the basis of this linearized description, the comparison of different proteins is possible at the levels of primary to tertiary structure. An application of the method to different cytochromes is reported here.
ASJC Scopus subject areas
- Condensed Matter Physics
- Physical and Theoretical Chemistry