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Journal Article|Research Support, N.I.H., Extramural |
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12313 |
| issn |
1520-4995
0006-2960 |
| issueIdentifier |
43 |
| pageRange |
12308-12313 |
| publicationName |
Biochemistry |
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12308 |
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| bibliographicCitation |
Aprilakis KN, Taskent H, Raleigh DP. Use of the novel fluorescent amino acid p-cyanophenylalanine offers a direct probe of hydrophobic core formation during the folding of the N-terminal domain of the ribosomal protein L9 and provides evidence for two-state folding. Biochemistry. 2007 Oct 30;46(43):12308–13. doi: 10.1021/bi7010674. PMID: 17924662. |
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http://rdf.ncbi.nlm.nih.gov/pubchem/author/MD5_e37de9b5752269f76b89d1fbc2a7618f |
| date |
2007-10-01-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| identifier |
https://pubmed.ncbi.nlm.nih.gov/17924662
https://doi.org/10.1021/bi7010674 |
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https://portal.issn.org/resource/ISSN/0006-2960
https://portal.issn.org/resource/ISSN/1520-4995 |
| language |
English |
| source |
https://pubmed.ncbi.nlm.nih.gov/
https://www.crossref.org/ |
| title |
Use of the Novel Fluorescent Amino Acidp-Cyanophenylalanine Offers a Direct Probe of Hydrophobic Core Formation during the Folding of the N-Terminal Domain of the Ribosomal Protein L9 and Provides Evidence for Two-State Folding |
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