{"database":"biostudies-literature","file_versions":[],"scores":{"citationCount":0,"reanalysisCount":0,"viewCount":58,"searchCount":0},"additional":{"omics_type":["Unknown"],"volume":["16(7)"],"submitter":["Goda N"],"pubmed_abstract":["Intrinsically disordered proteins (IDPs) that lack stable conformations and are highly flexible have attracted the attention of biologists. Therefore, the development of a systematic method to identify polypeptide regions that are unstructured in solution is important. We have designed an \"indirect/reflected\" detection system for evaluating the physicochemical properties of IDPs using nuclear magnetic resonance (NMR). This approach employs a \"chimeric membrane protein\"-based method using the thermostable membrane protein PH0471. This protein contains two domains, a transmembrane helical region and a C-terminal OB (oligonucleotide/oligosaccharide binding)-fold domain (named NfeDC domain), connected by a flexible linker. NMR signals of the OB-fold domain of detergent-solubilized PH0471 are observed because of the flexibility of the linker region. In this study, the linker region was substituted with target IDPs. Fifty-three candidates were selected using the prediction tool POODLE and 35 expression vectors were constructed. Subsequently, we obtained 15N-labeled chimeric PH0471 proteins with 25 IDPs as linkers. The NMR spectra allowed us to classify IDPs into three categories: flexible, moderately flexible, and inflexible. The inflexible IDPs contain membrane-associating or aggregation-prone sequences. This is the first attempt to use an indirect/reflected NMR method to evaluate IDPs and can verify the predictions derived from our computational tools."],"journal":["International journal of molecular sciences"],"pagination":["15743-60"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4519922"],"repository":["biostudies-literature"],"pubmed_title":["A Method for Systematic Assessment of Intrinsically Disordered Protein Regions by NMR."],"pmcid":["PMC4519922"],"pubmed_authors":["Goda N","Noguchi T","Kuwahara Y","Tenno T","Ota M","Hiroaki H","Ikegami T","Shimizu K"],"view_count":["58"],"additional_accession":[]},"is_claimable":false,"name":"A Method for Systematic Assessment of Intrinsically Disordered Protein Regions by NMR.","description":"Intrinsically disordered proteins (IDPs) that lack stable conformations and are highly flexible have attracted the attention of biologists. Therefore, the development of a systematic method to identify polypeptide regions that are unstructured in solution is important. We have designed an \"indirect/reflected\" detection system for evaluating the physicochemical properties of IDPs using nuclear magnetic resonance (NMR). This approach employs a \"chimeric membrane protein\"-based method using the thermostable membrane protein PH0471. This protein contains two domains, a transmembrane helical region and a C-terminal OB (oligonucleotide/oligosaccharide binding)-fold domain (named NfeDC domain), connected by a flexible linker. NMR signals of the OB-fold domain of detergent-solubilized PH0471 are observed because of the flexibility of the linker region. In this study, the linker region was substituted with target IDPs. Fifty-three candidates were selected using the prediction tool POODLE and 35 expression vectors were constructed. Subsequently, we obtained 15N-labeled chimeric PH0471 proteins with 25 IDPs as linkers. The NMR spectra allowed us to classify IDPs into three categories: flexible, moderately flexible, and inflexible. The inflexible IDPs contain membrane-associating or aggregation-prone sequences. This is the first attempt to use an indirect/reflected NMR method to evaluate IDPs and can verify the predictions derived from our computational tools.","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Jul","modification":"2024-11-13T02:58:30.81Z","creation":"2019-03-27T01:56:02Z"},"accession":"S-EPMC4519922","cross_references":{"pubmed":["26184172"],"doi":["10.3390/ijms160715743"]}}