Information Properties of Naturally-Occurring Proteins: Fourier Analysis and Complexity Phase Plots
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Abstract
In previous work from this lab, the information in natural proteins was investigated with Ribonuclease A (RNase A) serving as the source. The signature traits were investigated at three structure levels: primary through tertiary. The present paper travels further by charting the primary structure information of about half a million molecules. This was feasible given abundant sequence archives for both living and viral systems. Notably, a method is presented for evaluating primary structure information, based on Fourier analysis and spectral complexity. Significantly, the results show certain complexity traits to be universal for living sources. Viruses, by contrast, encode protein collections which are case-specific and complexity-divergent. The results have ramifications for discriminating collections on the basis of sequence information. This discrimination offers new strategies for selecting drug targets.
Keywords
Proteins Fourier analysis Spectral entropy Complexity Phase diagrams VirusesAbbreviations
- PDB
Protein data bank
- RNase A
Ribonuclease A
- QSAR
Quantitative structure activity relation
- CI
Correlated information
- WT
Wild type
- 2D
Two dimensional
Notes
Acknowledgments
The authors appreciate discussions with Professors Miguel Ballicora and Ken Olsen about individual proteins, natural libraries, and NCBI archives. The authors wish to thank an anonymous reviewer for comments and suggestions for improvement.
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