title: Beyond supersecondary structure: the global properties of protein sequences.
abstract: Analysis of the global properties of protein sequences, rather than single-site or local properties, has been shown to lead to new understanding of folding and function. Here we describe the use of software which can describe sequences numerically in an orthonormal fashion, Fourier-analyze those sequences, and verify the statistical significance of the resulting Fourier coefficients. The resulting parameters can be used to study problems involving sequences from a unique perspective.
authors.affiliation: Department of Pharmacology and Systems Therapeutics, Mount Sinai School of Medicine, New York University, New York, NY, USA. Shalom.Rackovsky@mssm.edu
authors.forename: S
authors.initials: S
authors.lastname: Rackovsky
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D019295:Computational Biology / Q000379:methods; D011506:Proteins / Q000737:chemistry*; D012984:Software
chemical_list: D011506:Proteins