{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,14]],"date-time":"2026-02-14T02:35:55Z","timestamp":1771036555053,"version":"3.50.1"},"reference-count":80,"publisher":"Public Library of Science (PLoS)","issue":"5","license":[{"start":{"date-parts":[[2007,5,25]],"date-time":"2007-05-25T00:00:00Z","timestamp":1180051200000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.ploscompbiol.org"],"crossmark-restriction":false},"short-container-title":["PLoS Comput Biol"],"DOI":"10.1371\/journal.pcbi.0030094","type":"journal-article","created":{"date-parts":[[2007,5,23]],"date-time":"2007-05-23T17:19:36Z","timestamp":1179940776000},"page":"e94","update-policy":"https:\/\/doi.org\/10.1371\/journal.pcbi.corrections_policy","source":"Crossref","is-referenced-by-count":42,"title":["Prediction of Functional Sites Based on the Fuzzy Oil Drop Model"],"prefix":"10.1371","volume":"3","author":[{"given":"Micha\u0142","family":"Bryli\u0144ski","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Katarzyna","family":"Prymula","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wiktor","family":"Jurkowski","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marek","family":"Kocha\u0144czyk","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ewa","family":"Stawowczyk","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Leszek","family":"Konieczny","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Irena","family":"Roterman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2007,5,25]]},"reference":[{"key":"pcbi-0030094-b001","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1038\/13783","article-title":"Structural genomics: Beyond the human genome project.","volume":"23","year":"1999","journal-title":"Nat Genet"},{"key":"pcbi-0030094-b002","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1110\/ps.4570102","article-title":"Structural genomics: A pipeline for providing structures for the biologist.","volume":"11","year":"2002","journal-title":"Protein Sci"},{"key":"pcbi-0030094-b003","doi-asserted-by":"crossref","first-page":"121","DOI":"10.2174\/1568005023342551","article-title":"The TB structural genomics consortium: Providing a structural foundation for drug discovery.","volume":"2","year":"2002","journal-title":"Curr Drug Targets Infect Disord"},{"key":"pcbi-0030094-b004","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1186\/gb-2004-5-9-343","article-title":"Structural genomics and structural biology: Compare and contrast.","volume":"5","year":"2004","journal-title":"Genome Biol"},{"key":"pcbi-0030094-b005","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1093\/protein\/2.2.127","article-title":"Analysis and prediction of the location of catalytic residues in enzymes.","volume":"2","year":"1988","journal-title":"Protein Eng"},{"key":"pcbi-0030094-b006","doi-asserted-by":"crossref","first-page":"2308","DOI":"10.1002\/pro.5560061104","article-title":"TESS: A geometric hashing algorithm for deriving 3D coordinate templates for searching structural databases. Application to enzyme active sites.","volume":"6","year":"1997","journal-title":"Protein Sci"},{"key":"pcbi-0030094-b007","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1006\/jmbi.1998.2144","article-title":"Predicting function: From genes to genomes and back.","volume":"283","year":"1998","journal-title":"J Mol Biol"},{"key":"pcbi-0030094-b008","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/S0167-7799(99)01398-0","article-title":"From genes to protein structure and function: Novel applications of computational approaches in the genomic era.","volume":"18","year":"2000","journal-title":"Trends Biotechnol"},{"key":"pcbi-0030094-b009","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1006\/jmbi.1999.2661","article-title":"The relationship between protein structure and function: A comprehensive survey with application to the yeast genome.","volume":"288","year":"1999","journal-title":"J Mol Biol"},{"key":"pcbi-0030094-b010","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1002\/1097-0134(20001001)41:1<98::AID-PROT120>3.0.CO;2-S","article-title":"Practical limits of function prediction.","volume":"41","year":"2000","journal-title":"Proteins"},{"key":"pcbi-0030094-b011","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1006\/jmbi.2000.3550","article-title":"Assessing annotation transfer for genomics: Quantifying the relations between protein sequence, structure and function through traditional and probabilistic scores.","volume":"297","year":"2000","journal-title":"J Mol Biol"},{"key":"pcbi-0030094-b012","doi-asserted-by":"crossref","first-page":"1884","DOI":"10.1002\/pro.5560070905","article-title":"Anatomy of protein pockets and cavities: Measurement of binding site geometry and implications for ligand design.","volume":"7","year":"1998","journal-title":"Protein Sci"},{"key":"pcbi-0030094-b013","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1007\/BF00124402","article-title":"Flexible ligand docking using a genetic algorithm.","volume":"9","year":"1995","journal-title":"J Comput Aided Mol Des"},{"key":"pcbi-0030094-b014","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1002\/1097-0134(20010215)42:3<296::AID-PROT20>3.0.CO;2-F","article-title":"Design, docking, and evaluation of multiple libraries against multiple targets.","volume":"42","year":"2001","journal-title":"Proteins"},{"key":"pcbi-0030094-b015","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1002\/prot.20448","article-title":"Does structural and chemical divergence play a role in precluding undesirable protein interactions?","volume":"59","year":"2005","journal-title":"Proteins"},{"key":"pcbi-0030094-b016","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1016\/0022-2836(92)90387-Y","article-title":"Effect of active site residues in barnase on activity and stability.","volume":"225","year":"1992","journal-title":"J Mol Biol"},{"key":"pcbi-0030094-b017","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1002\/prot.340130202","article-title":"Mutating the charged residues in the binding pocket of cellular retinoic acid-binding protein simultaneously reduces its binding affinity to retinoic acid and increases its thermostability.","volume":"13","year":"1992","journal-title":"Proteins"},{"key":"pcbi-0030094-b018","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1073\/pnas.92.2.452","article-title":"A relationship between protein stability and protein function.","volume":"92","year":"1995","journal-title":"Proc Natl Acad Sci U S A"},{"key":"pcbi-0030094-b019","doi-asserted-by":"crossref","first-page":"32729","DOI":"10.1074\/jbc.271.51.32729","article-title":"Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48.","volume":"271","year":"1996","journal-title":"J Biol Chem"},{"key":"pcbi-0030094-b020","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1006\/jmbi.2001.5009","article-title":"Prediction of functionally important residues based solely on the computed energetics of protein structure.","volume":"312","year":"2001","journal-title":"J Mol Biol"},{"key":"pcbi-0030094-b021","doi-asserted-by":"crossref","first-page":"12473","DOI":"10.1073\/pnas.211436698","article-title":"THEMATICS: A simple computational predictor of enzyme function from structure.","volume":"98","year":"2001","journal-title":"Proc Natl Acad Sci U S A"},{"key":"pcbi-0030094-b022","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1006\/jmbi.1997.1234","article-title":"Analysis of protein\u2013protein interaction sites using surface patches.","volume":"272","year":"1997","journal-title":"J Mol Biol"},{"key":"pcbi-0030094-b023","doi-asserted-by":"crossref","first-page":"127","DOI":"10.6026\/97320630001127","article-title":"Ligation site in proteins recognized in silico.","volume":"1","year":"2006","journal-title":"Bioinformation"},{"key":"pcbi-0030094-b024","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1080\/07391102.2006.10507076","article-title":"Fuzzy-oil-drop hydrophobic force field\u2014A model to represent late-stage folding (in silico) of lysozyme.","volume":"23","year":"2006","journal-title":"J Biomol Struct Dyn"},{"key":"pcbi-0030094-b025","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/j.compbiolchem.2006.04.007","article-title":"Hydrophobic collapse in (in silico) protein folding.","volume":"30","year":"2006","journal-title":"Comp Biol Chem"},{"key":"pcbi-0030094-b026","doi-asserted-by":"crossref","first-page":"1229","DOI":"10.1016\/j.biochi.2006.03.008","article-title":"Hydrophobic collapse in late-stage folding (in silico) of bovine pancreatic trypsin inhibitor.","volume":"88","year":"2006","journal-title":"Biochimie"},{"key":"pcbi-0030094-b027","first-page":"0002","article-title":"Gauss-function-based model of hydrophobicity density in proteins.","volume":"6","year":"2006","journal-title":"In Silico Biol"},{"key":"pcbi-0030094-b028","doi-asserted-by":"crossref","first-page":"7133","DOI":"10.1021\/bi00483a001","article-title":"Dominant forces in protein folding.","volume":"29","year":"1990","journal-title":"Biochemistry"},{"key":"pcbi-0030094-b029","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1096\/fasebj.10.1.8566551","article-title":"Forces contributing to the conformational stability of proteins.","volume":"10","year":"1996","journal-title":"FASEB J"},{"key":"pcbi-0030094-b030","doi-asserted-by":"crossref","first-page":"1657","DOI":"10.1126\/science.1069893","article-title":"Making a network of hydrophobic clusters.","volume":"295","year":"2002","journal-title":"Science"},{"key":"pcbi-0030094-b031","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/S0301-4622(03)00104-2","article-title":"Molecular and mesoscale structures in hydrophobically driven aqueous solutions.","volume":"105","year":"2003","journal-title":"Biophys Chem"},{"key":"pcbi-0030094-b032","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1016\/0003-9861(70)90401-7","article-title":"Comparison of molecular structures of proteins: Helix content; distribution of apolar residues.","volume":"138","year":"1970","journal-title":"Arch Biochem Biophys"},{"key":"pcbi-0030094-b033","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1016\/0005-2795(71)90271-6","article-title":"On the nature of the protein interior.","volume":"229","year":"1971","journal-title":"Biochim Biophys Acta"},{"key":"pcbi-0030094-b034","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1021\/ma60078a013","article-title":"Empirical studies of hydrophobicity. 1. Effect of protein size on the hydrophobic behavior of amino acids.","volume":"13","year":"1980","journal-title":"Macromolecules"},{"key":"pcbi-0030094-b035","doi-asserted-by":"crossref","first-page":"1406","DOI":"10.1021\/ma60078a014","article-title":"Empirical studies of hydrophobicity. 2. Distribution of the hydrophobic, hydrophilic, neutral, and ambivalent amino acids in the interior and exterior layers of native proteins.","volume":"13","year":"1980","journal-title":"Macromolecules"},{"key":"pcbi-0030094-b036","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1021\/ma50003a022","article-title":"Empirical studies of hydrophobicity. 3. Radial distribution of clusters of hydrophobic and hydrophilic amino acids.","volume":"14","year":"1981","journal-title":"Macromolecules"},{"key":"pcbi-0030094-b037","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0065-3233(08)60608-7","article-title":"Some factors in the interpretation of protein denaturation.","volume":"14","year":"1959","journal-title":"Adv Protein Chem"},{"key":"pcbi-0030094-b038","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1038\/254304a0","article-title":"Structural invariants in protein folding.","volume":"254","year":"1975","journal-title":"Nature"},{"key":"pcbi-0030094-b039","doi-asserted-by":"crossref","first-page":"4643","DOI":"10.1073\/pnas.77.8.4643","article-title":"Hydrophobic basis of packing in globular proteins.","volume":"77","year":"1980","journal-title":"Proc Natl Acad Sci U S A"},{"key":"pcbi-0030094-b040","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/0022-2836(82)90515-0","article-title":"A simple method for displaying the hydropathic character of a protein.","volume":"157","year":"1982","journal-title":"J Mol Biol"},{"key":"pcbi-0030094-b041","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1002\/prot.340040105","article-title":"Criteria that discriminate between native proteins and incorrectly folded models.","volume":"4","year":"1988","journal-title":"Proteins"},{"key":"pcbi-0030094-b042","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1093\/protein\/2.5.329","article-title":"Polarity as a criterion in protein design.","volume":"2","year":"1989","journal-title":"Protein Eng"},{"key":"pcbi-0030094-b043","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/0022-2836(92)91028-N","article-title":"Evaluation of protein models by atomic solvation preference.","volume":"225","year":"1992","journal-title":"J Mol Biol"},{"key":"pcbi-0030094-b044","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/1097-0134(20010401)43:1<1::AID-PROT1012>3.0.CO;2-A","article-title":"Improving the performance of Rosetta using multiple sequence alignment information and global measures of hydrophobic core formation.","volume":"43","year":"2001","journal-title":"Proteins"},{"key":"pcbi-0030094-b045","doi-asserted-by":"crossref","first-page":"9533","DOI":"10.1073\/pnas.93.18.9533","article-title":"Evidence for nonrandom hydrophobicity structures in protein chains.","volume":"93","year":"1996","journal-title":"Proc Natl Acad Sci U S A"},{"key":"pcbi-0030094-b046","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1111\/j.1399-3011.1978.tb02867.x","article-title":"A survey of atom packing in globular proteins.","volume":"12","year":"1978","journal-title":"Int J Pept Protein Res"},{"key":"pcbi-0030094-b047","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1111\/j.1399-3011.1979.tb01872.x","article-title":"Protein densities.","volume":"13","year":"1979","journal-title":"Int J Pept Protein Res"},{"key":"pcbi-0030094-b048","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1093\/bioinformatics\/btg391","article-title":"Limited conformational space for early-stage protein folding simulation.","volume":"20","year":"2004","journal-title":"Bioinformatics"},{"key":"pcbi-0030094-b049","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1002\/prot.20002","article-title":"Conformational subspace in simulation of early-stage protein folding.","volume":"55","year":"2004","journal-title":"Proteins"},{"key":"pcbi-0030094-b050","first-page":"65","article-title":"Early-stage folding in proteins (in silico) sequence-to-structure relation.","volume":"2","year":"2005","journal-title":"J Biomed Biotechnol"},{"key":"pcbi-0030094-b051","doi-asserted-by":"crossref","first-page":"D129","DOI":"10.1093\/nar\/gkh028","article-title":"The catalytic site atlas: A resource of catalytic sites and residues identified in enzymes using structural data.","volume":"32","year":"2004","journal-title":"Nucleic Acids Res"},{"key":"pcbi-0030094-b052","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1007\/s000180050069","article-title":"Annexin V interactions with collagen.","volume":"53","year":"1997","journal-title":"Cell Mol Life Sci"},{"key":"pcbi-0030094-b053","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1016\/j.sbi.2004.06.005","article-title":"Structure and mechanism of ABC transporters.","volume":"14","year":"2004","journal-title":"Curr Opin Struct Biol"},{"key":"pcbi-0030094-b054","unstructured":"DeLanoWL 2002 The PyMOL molecular graphics system Available: http:\/\/www.pymol.org. Accessed 14 February 2007."},{"key":"pcbi-0030094-b055","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/0022-2836(76)90004-8","article-title":"A simplified representation of protein conformations for rapid simulation of protein folding.","volume":"104","year":"1976","journal-title":"J Mol Biol"},{"key":"pcbi-0030094-b056","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/0022-2836(84)90309-7","article-title":"Analysis of membrane and surface protein sequences with the hydrophobic moment plot.","volume":"179","year":"1984","journal-title":"J Mol Biol"},{"key":"pcbi-0030094-b057","unstructured":"BrylinskiMKoniecznyLRotermanI 2007 Hydrophobic collapse: Late stage folding simulation of human \u03b1 and \u03b2 hemoglobin chains. Int J Bioinf Res Appl In press."},{"key":"pcbi-0030094-b058","doi-asserted-by":"crossref","unstructured":"JambonMAndrieuOCombetCDel\u00e9ageGDelfaudF 2006 The SuMo server: 3D search for protein functional sites. Bioinformatics 21 3929 3930","DOI":"10.1093\/bioinformatics\/bti645"},{"key":"pcbi-0030094-b059","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1002\/prot.10339","article-title":"A new bioinformatic approach to detect common 3D sites in protein structures.","volume":"52","year":"2003","journal-title":"Proteins"},{"key":"pcbi-0030094-b060","doi-asserted-by":"crossref","first-page":"W89","DOI":"10.1093\/nar\/gki414","article-title":"ProFunc: A server for predicting protein function from 3D structure.","volume":"33","year":"2005","journal-title":"Nucleic Acids Res"},{"key":"pcbi-0030094-b061","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1016\/j.jmb.2005.05.067","article-title":"Protein function prediction using local 3D templates.","volume":"351","year":"2005","journal-title":"J Mol Biol"},{"key":"pcbi-0030094-b062","first-page":"107","article-title":"Annexin V-crystal structure and its implications on function.","volume":"91","year":"1992","journal-title":"Behring Inst Mitt"},{"key":"pcbi-0030094-b063","doi-asserted-by":"crossref","first-page":"8429","DOI":"10.1074\/jbc.M212239200","article-title":"Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding.","volume":"278","year":"2003","journal-title":"J Biol Chem"},{"key":"pcbi-0030094-b064","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/S0079-6107(00)00003-1","article-title":"Biophysical and molecular properties of annexin-formed channels.","volume":"73","year":"2000","journal-title":"Prog Biophys Mol Biol"},{"key":"pcbi-0030094-b065","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1016\/j.jmb.2004.10.055","article-title":"Network analysis of protein structures identifies functional residues.","volume":"344","year":"2004","journal-title":"J Mol Biol"},{"key":"pcbi-0030094-b066","doi-asserted-by":"crossref","first-page":"1908","DOI":"10.1093\/bioinformatics\/bti315","article-title":"Q-SiteFinder: An energy-based method for the prediction of protein-ligand binding sites.","volume":"21","year":"2005","journal-title":"Bioinformatics"},{"key":"pcbi-0030094-b067","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1007\/BF02174466","article-title":"SPROUT, HIPPO and CAESA: Tools for de novo structure generation and estimation of synthetic accessibility.","volume":"3","year":"1995","journal-title":"Perspect Drug Discov Design"},{"key":"pcbi-0030094-b068","doi-asserted-by":"crossref","unstructured":"LawJMSFungDYKZsoldosZSimonASzaboZ 2003 Validation of the SPROUT de novo design program. J Mol Struct THEOCHEM 651 657 Additional pages: 666-667","DOI":"10.1016\/j.theochem.2003.08.104"},{"key":"pcbi-0030094-b069","unstructured":"WeiLAltmanRB 1998 Recognizing protein binding sites using statistical descriptions of their 3D environments. Pac Symp Biocomput 497 508"},{"key":"pcbi-0030094-b070","doi-asserted-by":"crossref","first-page":"3324","DOI":"10.1093\/nar\/gkg553","article-title":"WebFEATURE: An interactive web tool for identifying and visualizing functional sites on macromolecular structures.","volume":"31","year":"2003","journal-title":"Nucleic Acids Res"},{"key":"pcbi-0030094-b071","doi-asserted-by":"crossref","first-page":"4450","DOI":"10.1093\/nar\/gkg471","article-title":"Microenvironment analysis and identification of magnesium binding sites in RNA.","volume":"31","year":"2003","journal-title":"Nucleic Acids Res"},{"issue":"Supplement 1","key":"pcbi-0030094-b072","first-page":"i258","article-title":"Prediction of active sites for protein structures from computed chemical properties.","volume":"21","year":"2005","journal-title":"Bioinformatics"},{"key":"pcbi-0030094-b073","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1142\/S0219720005000916","article-title":"Active site prediction for comparative model structures with thematics.","volume":"3","year":"2005","journal-title":"J Bioinform Comput Biol"},{"key":"pcbi-0030094-b074","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1002\/prot.20418","article-title":"Statistical criteria for the identification of protein active sites using theoretical microscopic titration curves.","volume":"59","year":"2005","journal-title":"Proteins"},{"key":"pcbi-0030094-b075","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1006\/jmbi.1996.0077","article-title":"The automatic search for ligand binding sites in proteins of known three-dimensional structure using only geometric criteria.","volume":"256","year":"1996","journal-title":"J Mol Biol"},{"key":"pcbi-0030094-b076","first-page":"31","article-title":"Comprehensive identification of druggable protein ligand binding sites.","volume":"15","year":"2004","journal-title":"Genome Inform"},{"key":"pcbi-0030094-b077","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1016\/S1093-3263(98)00002-3","article-title":"LIGSITE: Automatic and efficient detection of potential small molecule-binding sites in proteins.","volume":"15","year":"1997","journal-title":"J Mol Graph Model"},{"key":"pcbi-0030094-b078","doi-asserted-by":"crossref","first-page":"5361","DOI":"10.1073\/pnas.0509355103","article-title":"Physically realistic homology models built with ROSETTA can be more accurate than their templates.","volume":"103","year":"2006","journal-title":"Proc Natl Acad Sci U S A"},{"key":"pcbi-0030094-b079","first-page":"827","article-title":"Investigation of de novo totally random biosequences. Part I: A general method for in vitro selection of folded domains from a random polypeptide library displayed on phage.","volume":"3","year":"2006","journal-title":"Chem Biodivers"},{"key":"pcbi-0030094-b080","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1002\/cbdv.200690088","article-title":"Investigation of de novo totally random biosequences, Part II: On the folding frequency in a totally random library of de novo proteins obtained by phage display.","volume":"3","year":"2006","journal-title":"Chem Biodivers"}],"container-title":["PLoS Computational Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pcbi.0030094","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,2,14]],"date-time":"2024-02-14T13:05:25Z","timestamp":1707915925000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pcbi.0030094"}},"subtitle":[],"editor":[{"given":"Philip E","family":"Bourne","sequence":"first","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2007,5,25]]},"references-count":80,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2007,5,25]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pcbi.0030094","relation":{},"ISSN":["1553-7358"],"issn-type":[{"value":"1553-7358","type":"electronic"}],"subject":[],"published":{"date-parts":[[2007,5,25]]}}}