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Updated: Jul 19, 2026

Tools to Study the Role of Architectural Protein HMGB1 in the Processing of Helix Distorting, Site-specific DNA Interstrand Crosslinks
Published on: November 10, 2016
Characterization of architecture signals in proteins
1Department 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
Abstract:
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.
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