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Protein structure analysis using the resonant recognition model and wavelet transforms.

作者信息

Fang Q, Cosic I

机构信息

Department of Electrical and Computer System Engineering Monash University, Caulfield East Vic.

出版信息

Australas Phys Eng Sci Med. 1998 Dec;21(4):179-85.

PMID:10050348
Abstract

An approach based on the resonant recognition model and the discrete wavelet transform is introduced here for characterising proteins' biological function. The protein sequence is converted into a numerical series by assigning the electron-ion interaction potential to each amino acid from N-terminal to C-terminal. A set of peaks is found after performing a wavelet transform onto a numerical series representing a group of homologous proteins. These peaks are related to protein structural and functional properties and named characteristic vector of that protein group. Further more, the amino acids contributing mostly to a protein's biological functions, the so-called 'hot spots' amino acids, are predicted by the continuous wavelet transform. It is found that the hot spots are clustered around the protein's cleft structure. The wavelets approach provides a novel methods for amino acid sequence analysis as well as an expansion for the newly established macromolecular interaction model: the resonant recognition model.

摘要

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