2007 journal article

Application of complex demodulation on bZIP and bHLH-PAS protein domains

Mathematical Biosciences, 207(2), 204–218.

By: Z. Wang n, C. Smith n & W. Atchley n

MeSH headings : Algorithms; Amino Acid Motifs; Amino Acid Sequence; Aryl Hydrocarbon Receptor Nuclear Translocator / chemistry; Basic Helix-Loop-Helix Transcription Factors / chemistry; Basic-Leucine Zipper Transcription Factors / chemistry; Computational Biology / methods; Databases, Protein; Entropy; Factor Analysis, Statistical; Fourier Analysis; Humans; Molecular Sequence Data; Protein Structure, Secondary; Protein Structure, Tertiary; Proto-Oncogene Proteins c-fos / chemistry
TL;DR: This work analyzed bZIP and bHLH-PAS protein domains and introduced complex demodulation (CDM) to detect functional regions in protein sequences data and found that the local amplitude minimum or local amplitude maximum of the 3.6-aa periodic component is associated with protein structural or functional information. (via Semantic Scholar)
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Source: NC State University Libraries
Added: August 6, 2018

Proteins are built with molecular modular building blocks such as an alpha-helix, beta-sheet, loop region and other structures. This is an economical way of constructing complex molecules. Periodicity analysis of protein sequences has allowed us to obtain meaningful information concerning their structure, function and evolution. In this work, complex demodulation (CDM) is introduced to detect functional regions in protein sequences data. More specifically, we analyzed bZIP and bHLH-PAS protein domains. Complex demodulation provided insightful information about changing amplitudes of periodic components in protein sequences. Furthermore, it was found that the local amplitude minimum or local amplitude maximum of the 3.6-aa periodic component is associated with protein structural or functional information due to the observation that the extrema are mainly located in the boundary area of two structural or functional regions.