DC Field | Value | Language |
---|---|---|
dc.contributor.author | Yi, Gwan-Su | ko |
dc.contributor.author | Choi, Byong-Seok | ko |
dc.contributor.author | Kim, Hyoung Man | ko |
dc.date.accessioned | 2013-02-25T21:20:27Z | - |
dc.date.available | 2013-02-25T21:20:27Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 1994-05 | - |
dc.identifier.citation | BIOPHYSICAL JOURNAL, v.66, no.5, pp.1604 - 1611 | - |
dc.identifier.issn | 0006-3495 | - |
dc.identifier.uri | http://hdl.handle.net/10203/65371 | - |
dc.description.abstract | The structure of a chemically synthesized 25-residue-long functional signal peptide of Escherichia coli ribose binding protein was compared with that of a nonfunctional mutant-signal peptide using circular dichroism and two-dimensional H-1 NMR in solvents mimicking the amphiphilic environments. The functional peptide forms an 18-residue-long alpha-helix starting from the NH2-terminal region and reaching to the hydrophobic stretch in a solvent consisting of 10% dimethylsulfoxide, 40% water, and 50% trifluoroethanol (v/v). The nonfunctional mutant peptide, which contains a Pro at position 9 instead of a Leu in the wild-type peptide, does not have any secondary structure in that solvent but forms a 12-residue-long alpha-helix within the hydrophobic stretch in water/trifluoroethanol (50:50, v/v) solvent. It seems that the Pro-9 residue in the nonfunctional peptide disturbs the helix propagation from the hydrophobic stretch to the NH2-terminal region. Because both of these peptides have stable helices within the hydrophobic stretch, it may be concluded that the additional 2 turns of the alpha-helix in the NH2-terminal region of the wild-type signal peptide is important for its function. | - |
dc.language | English | - |
dc.publisher | BIOPHYSICAL SOCIETY | - |
dc.subject | NUCLEAR-MAGNETIC-RESONANCE | - |
dc.subject | PROTON PROTON DISTANCES | - |
dc.subject | CIRCULAR-DICHROISM | - |
dc.subject | H-1-NMR SPECTRA | - |
dc.subject | SPECTROSCOPY | - |
dc.subject | CONFORMATION | - |
dc.subject | PEPTIDES | - |
dc.subject | STABILITY | - |
dc.subject | EXPORT | - |
dc.subject | MODEL | - |
dc.title | STRUCTURES OF WILD-TYPE AND MUTANT SIGNAL SEQUENCES OF ESCHERICHIA-COLI RIBOSE BINDING-PROTEIN | - |
dc.type | Article | - |
dc.identifier.wosid | A1994NG92300037 | - |
dc.identifier.scopusid | 2-s2.0-0028218962 | - |
dc.type.rims | ART | - |
dc.citation.volume | 66 | - |
dc.citation.issue | 5 | - |
dc.citation.beginningpage | 1604 | - |
dc.citation.endingpage | 1611 | - |
dc.citation.publicationname | BIOPHYSICAL JOURNAL | - |
dc.contributor.localauthor | Yi, Gwan-Su | - |
dc.contributor.localauthor | Choi, Byong-Seok | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | NUCLEAR-MAGNETIC-RESONANCE | - |
dc.subject.keywordPlus | PROTON PROTON DISTANCES | - |
dc.subject.keywordPlus | CIRCULAR-DICHROISM | - |
dc.subject.keywordPlus | H-1-NMR SPECTRA | - |
dc.subject.keywordPlus | SPECTROSCOPY | - |
dc.subject.keywordPlus | CONFORMATION | - |
dc.subject.keywordPlus | PEPTIDES | - |
dc.subject.keywordPlus | STABILITY | - |
dc.subject.keywordPlus | EXPORT | - |
dc.subject.keywordPlus | MODEL | - |
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