title: Sequence determinants of protein architecture.
abstract: Delineation of the relationship between sequence and structure in proteins has proven elusive. Most studies of this problem use alignment methods and other approaches based on the characteristics of individual residues. It is demonstrated herein that the sequence-structure relationship is determined in significant part by global characteristics of sequence organization. Information encoded in complete sequences is required to distinguish proteins in different architectural groups. It is found that the statistically significant differences between sequences encoding different architectures are encoded in a surprisingly small set of low-wave-number sequence periodicities. It would therefore appear that unexpected simplicity in an appropriately defined Fourier space may be an inherent characteristic of the sequences of folded proteins.
authors.affiliation: Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, 14853.
authors.forename: S
authors.initials: S
authors.lastname: Rackovsky
mesh_terms: D019295:Computational Biology / Q000379:methods; D016208:Databases, Factual; D005583:Fourier Analysis; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D020539:Sequence Analysis, Protein / Q000379:methods*
chemical_list: D011506:Proteins
keywords: Fourier analysis; distant homologies; fold detection; protein folding; sequence-structure relationships