OBJECTIVES: A wavelet based approach for the hydrophobicity analysis of protein primary structures is proposed to predict the presence of alpha helices in the secondary structure. METHODS: The information about hydropathy profile periodicity content together with a score of probability of occurrence of a single amino acid allows the localization of alpha helices. RESULTS: The accuracy is comparable to other consolidated predictors based on different techniques (i.e.: neural networks, hidden markov models). CONCLUSION: This method is particularly suitable to capture the amphiphilic character of the helical structures.
Keywords: Protein sequence, secondary structure, hydrophobicity, alpha helix, wavelet transform
01/2004 | Methods of Information in Medicine, SchattauerIn structural deformation analysis the behaviour of the monitored structure is typically described in a dynamic model, by deducing a weighting or transfer function...
Keywords: Change-points, Maximum-likelihood, wavelet transform
09/2007 | Journal of Applied Geodesy, Walter de Gruyter