| http://purl.uniprot.org/citations/33535444 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/33535444 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/33535444 | http://www.w3.org/2000/01/rdf-schema#comment | "Uniformly 13C- and 15N-labeled samples ensure fast and reliable nuclear magnetic resonance (NMR) assignments of proteins and are commonly used for structure elucidation by NMR. However, the preparation of uniformly labeled samples is a labor-intensive and expensive step. Reducing the portion of 13C-labeled glucose by a factor of five using a fractional 20% 13C- and 100% 15N-labeling scheme could lower the total chemical costs, yet retaining sufficient structural information of uniformly [13C, 15N]-labeled sample as a result of the improved sensitivity of NMR instruments. Moreover, fractional 13C-labeling can facilitate reliable resonance assignments of sidechains because of the biosynthetic pathways of each amino-acid. Preparation of only one [20% 13C, 100% 15N]-labeled sample for small proteins (<15 kDa) could also eliminate redundant sample preparations of 100% 15N-labeled and uniformly 100% [13C, 15N]-labeled samples of proteins. We determined the NMR structures of a small alpha-helical protein, the C domain of IgG-binding protein A from Staphylococcus aureus (SpaC), and a small beta-sheet protein, CBM64 module using [20% 13C, 100% 15N]-labeled sample and compared with the crystal structures and the NMR structures derived from the 100% [13C, 15N]-labeled sample. Our results suggest that one [20% 13C, 100% 15N]-labeled sample of small proteins could be routinely used as an alternative to conventional 100% [13C, 15N]-labeling for backbone resonance assignments, NMR structure determination, 15N-relaxation analysis, and ligand-protein interaction."xsd:string |
| http://purl.uniprot.org/citations/33535444 | http://purl.org/dc/terms/identifier | "doi:10.3390/molecules26030747"xsd:string |
| http://purl.uniprot.org/citations/33535444 | http://purl.org/dc/terms/identifier | "doi:10.3390/molecules26030747"xsd:string |
| http://purl.uniprot.org/citations/33535444 | http://purl.uniprot.org/core/author | "Iwai H."xsd:string |
| http://purl.uniprot.org/citations/33535444 | http://purl.uniprot.org/core/author | "Iwai H."xsd:string |
| http://purl.uniprot.org/citations/33535444 | http://purl.uniprot.org/core/author | "Heikkinen H.A."xsd:string |
| http://purl.uniprot.org/citations/33535444 | http://purl.uniprot.org/core/author | "Heikkinen H.A."xsd:string |
| http://purl.uniprot.org/citations/33535444 | http://purl.uniprot.org/core/author | "Backlund S.M."xsd:string |
| http://purl.uniprot.org/citations/33535444 | http://purl.uniprot.org/core/author | "Backlund S.M."xsd:string |
| http://purl.uniprot.org/citations/33535444 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
| http://purl.uniprot.org/citations/33535444 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
| http://purl.uniprot.org/citations/33535444 | http://purl.uniprot.org/core/name | "Molecules"xsd:string |
| http://purl.uniprot.org/citations/33535444 | http://purl.uniprot.org/core/name | "Molecules"xsd:string |
| http://purl.uniprot.org/citations/33535444 | http://purl.uniprot.org/core/pages | "747"xsd:string |
| http://purl.uniprot.org/citations/33535444 | http://purl.uniprot.org/core/title | "NMR Structure Determinations of Small Proteins Using only One Fractionally 20% 13C- and Uniformly 100% 15N-Labeled Sample."xsd:string |
| http://purl.uniprot.org/citations/33535444 | http://purl.uniprot.org/core/title | "NMR Structure Determinations of Small Proteins Using only One Fractionally 20% 13C- and Uniformly 100% 15N-Labeled Sample."xsd:string |
| http://purl.uniprot.org/citations/33535444 | http://purl.uniprot.org/core/volume | "26"xsd:string |
| http://purl.uniprot.org/citations/33535444 | http://purl.uniprot.org/core/volume | "26"xsd:string |
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