{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["101(24)"],"submitter":["Ivankov DN"],"pubmed_abstract":["We present a method for predicting folding rates of proteins from their amino acid sequences only, or rather, from their chain lengths and their helicity predicted from their sequences. The method achieves 82% correlation with experiment over all 64 \"two-state\" and \"multistate\" proteins (including two artificial peptides) studied up to now."],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pagination":["8942-4"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC428451"],"repository":["biostudies-literature"],"pubmed_title":["Prediction of protein folding rates from the amino acid sequence-predicted secondary structure."],"pmcid":["PMC428451"],"pubmed_authors":["Ivankov DN","Finkelstein AV"],"additional_accession":[]},"is_claimable":false,"name":"Prediction of protein folding rates from the amino acid sequence-predicted secondary structure.","description":"We present a method for predicting folding rates of proteins from their amino acid sequences only, or rather, from their chain lengths and their helicity predicted from their sequences. The method achieves 82% correlation with experiment over all 64 \"two-state\" and \"multistate\" proteins (including two artificial peptides) studied up to now.","dates":{"release":"2004-01-01T00:00:00Z","publication":"2004 Jun","modification":"2024-11-07T04:05:49.472Z","creation":"2019-03-27T00:50:32Z"},"accession":"S-EPMC428451","cross_references":{"pubmed":["15184682"],"doi":["10.1073/pnas.0402659101"]}}