Characterization of architecture signals in proteins.
A quantitative, property-based approach to protein sequence analysis is presented, grounded in Fourier analysis and signal-processing methodologies. The resulting tools are applied to four protein structure families. We demonstrate the existence of architecture-specific, large amplitude periodicities in amino acid properties encoded in the sequences of proteins. These signals, whose statistical significance we establish, occur at well-defined wavenumbers, but are expressed in different physical properties in the various proteins which fold to a common architecture. This result explains the long-known convergence of unrelated sequences to a common fold. It is further suggested that these results provide a physical basis for the experimental observation that unrelated sequences that adopt similar architectures fold with similar rates.
Rackovsky
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Department of Pharmacology and Biological Chemistry and Center for Biomathematical Sciences, Mount Sinai School of Medicine, One Gustave L. Levy Place, New York, New York 10029, USA. shelly@camelot.mssm.edu
D000595:Amino Acid Sequence; D005583:Fourier Analysis; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
D011506:Proteins