Accessibility of folding mutation sites in the native phage p22 tailspike protein trimer

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dc.contributor.authorM BeiBinger-
dc.contributor.authorMyeong Hee Yu-
dc.contributor.authorR Seckler-
dc.date.accessioned2017-04-19T08:53:57Z-
dc.date.available2017-04-19T08:53:57Z-
dc.date.issued1994-
dc.identifier.issn0929-8665-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/3987-
dc.description.abstractCystein substitutions at sites of 3 temperature-sensitive-folding (tsf) and 2 tsf-suppressor mutations in the phage P22 tailspike protein were created in order to probe the solvent accessibility of these sites. Cysteines at 2 tsf sites (residues 235 and 244) reacted readily with Ellman's reagent and labeled by fluorescent maleimides. Spectra of the labeled proteins indicated the electrostatic enviornment of the 2 sites to be different. The 2 suppressor sites (residues 331 and 334) and residue 238 were inaccessible to the reagents.-
dc.publisherBentham Science Publ Ltd-
dc.titleAccessibility of folding mutation sites in the native phage p22 tailspike protein trimer-
dc.title.alternativeAccessibility of folding mutation sites in the native phage p22 tailspike protein trimer-
dc.typeArticle-
dc.citation.titleProtein and Peptide Letters-
dc.citation.number1-
dc.citation.endPage4-
dc.citation.startPage1-
dc.citation.volume1-
dc.contributor.affiliatedAuthorMyeong Hee Yu-
dc.contributor.alternativeNameBeiBinger-
dc.contributor.alternativeName유명희-
dc.contributor.alternativeNameSeckler-
dc.identifier.bibliographicCitationProtein and Peptide Letters, vol. 1, no. 1, pp. 1-4-
dc.description.journalClassY-
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