{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,7]],"date-time":"2025-11-07T08:43:13Z","timestamp":1762504993697},"reference-count":40,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2004,11,30]],"date-time":"2004-11-30T00:00:00Z","timestamp":1101772800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/2.0\/"},{"start":{"date-parts":[[2004,11,30]],"date-time":"2004-11-30T00:00:00Z","timestamp":1101772800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/2.0\/"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["BMC Bioinformatics"],"abstract":"<jats:title>Abstract<\/jats:title><jats:sec>\n                        <jats:title>Background<\/jats:title>\n                        <jats:p>The protein structure prediction problem is one of the most challenging problems in biological sciences. Many approaches have been proposed using database information and\/or simplified protein models. The protein structure prediction problem can be cast in the form of an optimization problem. Notwithstanding its importance, the problem has very seldom been tackled by Constraint Logic Programming, a declarative programming paradigm suitable for solving combinatorial optimization problems.<\/jats:p>\n                     <\/jats:sec><jats:sec>\n                        <jats:title>Results<\/jats:title>\n                        <jats:p>Constraint Logic Programming techniques have been applied to the protein structure prediction problem on the face-centered cube lattice model. Molecular dynamics techniques, endowed with the notion of constraint, have been also exploited. Even using a very simplified model, Constraint Logic Programming on the face-centered cube lattice model allowed us to obtain acceptable results for a few small proteins. As a test implementation their (known) secondary structure and the presence of disulfide bridges are used as constraints. Simplified structures obtained in this way have been converted to all atom models with plausible structure. Results have been compared with a similar approach using a well-established technique as molecular dynamics.<\/jats:p>\n                     <\/jats:sec><jats:sec>\n                        <jats:title>Conclusions<\/jats:title>\n                        <jats:p>The results obtained on small proteins show that Constraint Logic Programming techniques can be employed for studying protein simplified models, which can be converted into realistic all atom models. The advantage of Constraint Logic Programming over other, much more explored, methodologies, resides in the rapid software prototyping, in the easy way of encoding heuristics, and in exploiting all the advances made in this research area, e.g. in constraint propagation and its use for pruning the huge search space.<\/jats:p>\n                     <\/jats:sec>","DOI":"10.1186\/1471-2105-5-186","type":"journal-article","created":{"date-parts":[[2005,1,13]],"date-time":"2005-01-13T09:24:41Z","timestamp":1105608281000},"update-policy":"http:\/\/dx.doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":42,"title":["Constraint Logic Programming approach to protein structure prediction"],"prefix":"10.1186","volume":"5","author":[{"given":"Alessandro","family":"Dal Pal\u00f9","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Agostino","family":"Dovier","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Federico","family":"Fogolari","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2004,11,30]]},"reference":[{"doi-asserted-by":"crossref","unstructured":"Moult J, Hubbard T, Fidelis K, Pedersen J: Critical Assessment of Methods of Protein Structure Prediction (CASP): Round III.\n                           Proteins: Struct Funct Genet 1999, (Suppl 3):2\u20136.","key":"302_CR1","DOI":"10.1002\/(SICI)1097-0134(1999)37:3+<2::AID-PROT2>3.0.CO;2-2"},{"doi-asserted-by":"crossref","unstructured":"Venclovas C, Zemla A, Fidelis K, Moult J: Assessment of progress over the CASP experiments.\n                           Proteins: Struct Funct Genet 2003, (Suppl 6):585\u2013595.","key":"302_CR2","DOI":"10.1002\/prot.10530"},{"key":"302_CR3","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1093\/nar\/28.1.235","volume":"28","author":"HM Berman","year":"2000","unstructured":"Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank.\n                           Nucleic Acids Res 2000, 28: 235\u2013242.","journal-title":"Nucleic Acids Res"},{"key":"302_CR4","doi-asserted-by":"publisher","first-page":"511","DOI":"10.1016\/j.polymer.2003.10.064","volume":"45","author":"J Skolnick","year":"2004","unstructured":"Skolnick J, Kolinski A: Reduced models of proteins and their applications.\n                           Polymer 2004, 45: 511\u2013524.","journal-title":"Polymer"},{"key":"302_CR5","doi-asserted-by":"publisher","first-page":"199","DOI":"10.1016\/0022-2836(87)90521-3","volume":"196","author":"D Bashford","year":"1987","unstructured":"Bashford D, Chothia C, Lesk A: Determinants of a protein fold. 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