Information properties of naturally-occurring proteins: Fourier analysis and complexity phase plots.
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.
Department of Chemistry, Loyola University Chicago, 6525 North Sheridan Road, Chicago, IL 60626, USA. dgraha1@luc.edu
Daniel J
DJ
Graham
Shelby
S
Grzetic
Donald
D
May
John
J
Zumpf
D000595:Amino Acid Sequence; D019277:Entropy; D029968:Escherichia coli Proteins / Q000737:chemistry; D005583:Fourier Analysis; D007536:Isomerism; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D020539:Sequence Analysis, Protein; D014764:Viral Proteins / Q000737:chemistry
D029968:Escherichia coli Proteins; D011506:Proteins; D014764:Viral Proteins