{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,7]],"date-time":"2025-11-07T08:45:39Z","timestamp":1762505139261},"reference-count":31,"publisher":"Oxford University Press (OUP)","issue":"15","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2006,8,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Motivation: Conformational flexibility is essential to the function of many proteins, e.g. catalytic activity. To assist efforts in determining and exploring the functional properties of a protein, it is desirable to automatically identify regions that are prone to undergo conformational changes. It was recently shown that a probabilistic predictor of continuum secondary structure is more accurate than categorical predictors for structurally ambivalent sequence regions, suggesting that such models are suited to characterize protein flexibility.<\/jats:p>\n               <jats:p>Results: We develop a computational method for identifying regions that are prone to conformational change directly from the amino acid sequence. The method uses the entropy of the probabilistic output of an 8-class continuum secondary structure predictor. Results for 171 unique amino acid sequences with well-characterized variable structure (identified in the \u2018Macromolecular movements database\u2019) indicate that the method is highly sensitive at identifying flexible protein regions, but false positives remain a problem. The method can be used to explore conformational flexibility of proteins (including hypothetical or synthetic ones) whose structure is yet to be determined experimentally.<\/jats:p>\n               <jats:p>Availability: The predictor, sequence data and supplementary studies are available at and are free for academic use.<\/jats:p>\n               <jats:p>Contact: \u00a0mikael@itee.uq.edu.au<\/jats:p>","DOI":"10.1093\/bioinformatics\/btl198","type":"journal-article","created":{"date-parts":[[2006,5,24]],"date-time":"2006-05-24T03:34:28Z","timestamp":1148441668000},"page":"1809-1814","source":"Crossref","is-referenced-by-count":15,"title":["Identifying sequence regions undergoing conformational change via predicted continuum secondary structure"],"prefix":"10.1093","volume":"22","author":[{"given":"Mikael","family":"Bod\u00e9n","sequence":"first","affiliation":[{"name":"School of Information Technology and Electrical Engineering, QLD 4072, The University of Queensland 1 \u00a0 1 \u00a0 \u00a0 Australia"}]},{"given":"Timothy L.","family":"Bailey","sequence":"additional","affiliation":[{"name":"Institute for Molecular Bioscience, QLD 4072, The University of Queensland 2 \u00a0 2 \u00a0 \u00a0 Australia"}]}],"member":"286","published-online":{"date-parts":[[2006,5,23]]},"reference":[{"key":"2023012409112282800_b1","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1110\/ps.04882105","article-title":"Normal modes for predicting protein motions: a comprehensive database assessment and associated web tool","volume":"14","author":"Alexandrov","year":"2005","journal-title":"Protein Sci."},{"key":"2023012409112282800_b2","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/S0969-2126(02)00700-1","article-title":"Continuum secondary structure captures protein flexibility","volume":"10","author":"Andersen","year":"2002","journal-title":"Structure"},{"key":"2023012409112282800_b3","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1093\/bioinformatics\/16.5.412","article-title":"Assessing the accuracy of prediction algorithms for classification: an overview","volume":"16","author":"Baldi","year":"2000","journal-title":"Bioinformatics"},{"key":"2023012409112282800_b4","doi-asserted-by":"crossref","first-page":"14970","DOI":"10.1021\/ja054842f","article-title":"A simple method to predict protein flexibility using secondary chemical shifts","volume":"127","author":"Berjanskii","year":"2005","journal-title":"J. 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