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Journal of the American Chemical Society
Volumn 130, Issue 51, 2008, Pages 17384-17393
Pathway for unfolding of ubiquitin in sodium dodecyl sulfate, studied by capillary electrophoresis
Author keywords

[No Author keywords available]
Indexed keywords

AMIDE HYDROGENS; BIOPHYSICAL METHODS; CD SPECTROSCOPY; CHARGED SURFACTANTS; CHEMICAL COMPOSITIONS; CIRCULAR DICHROISM; CONCENTRATION OF; FOUR-GROUP; HELICAL CONTENT; KEY CHARACTERISTICS; LEVEL OF DETAIL; MASS SPECTROSCOPY; NEW TOOLS; SDS-POLYACRYLAMIDE GEL ELECTROPHORESIS; SODIUM DODECYL SULFATE; UBIQUITIN;
EID: 67749137430     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja804736t     Document Type: Article
Times cited : (41)
References (55)
  • 4
    • 20744442020 scopus 로고    scopus 로고
    • Dill, K, A.; Truskett, T. M.; Vlachv. V.; Hribar-Lee, B. Annu. Rev. Biophys. Biomol Struct. 2005, 34. 173-199.
    • Dill, K, A.; Truskett, T. M.; Vlachv. V.; Hribar-Lee, B. Annu. Rev. Biophys. Biomol Struct. 2005, 34. 173-199.
  • 6
    • 67849135265 scopus 로고    scopus 로고
    • Gudiksen. K. L.; Gitlin, 1.; Moustakas. D. T.; Whitesides, G. M. Biophys. J. 2006, 91, 298-310.
    • Gudiksen. K. L.; Gitlin, 1.; Moustakas. D. T.; Whitesides, G. M. Biophys. J. 2006, 91, 298-310.
  • 38
    • 67849105775 scopus 로고    scopus 로고
    • We did not account for the sodium ion in SDS for these corrections, as only the dodecyl sulfate moieties DS, associate with UBI; Na+is the counterion
    • +is the counterion.
  • 41
    • 84869564403 scopus 로고    scopus 로고
    • Figure S5 in the Supporting Information provides the SDS-PAGE analysis of ten proteins with molecular weights from 2.5 to 20 kDa, including UBI (equilibrated against both 10 and 30 mM SDS and denatured at both 22 and 100 °C). On the basis of the SDS-PAGE results, it is reasonable to conclude that D is fully denatured and saturated with SDS at the ratio of 1.4 g of SDS per gram of protein.
    • Figure S5 in the Supporting Information provides the SDS-PAGE analysis of ten proteins with molecular weights from 2.5 to 20 kDa, including UBI (equilibrated against both 10 and 30 mM SDS and denatured at both 22 and 100 °C). On the basis of the SDS-PAGE results, it is reasonable to conclude that D is fully denatured and saturated with SDS at the ratio of 1.4 g of SDS per gram of protein.
  • 42
    • 84869574814 scopus 로고    scopus 로고
    • At [SDS] > 2.8 mM, a peak appears at μ < 1.2 cm2 kV-L min-1, directly after the neutral marker (DMF) peak (Figure la,d, We bserved the same peak under similar conditions when only DMF was injected (see Supporting Information, Figures S3a and S8, We hypothesize that this signal arises from the partitioning of an impurity within SDS micelles (Figure 1, cmc labeled with a dotted bracket, To verify this hypothesis, we analyzed injections of a UV-absorbent hydrophobic marker into the buffer (20 μM of 2-hydroxymethyl-enenaphthalene, Figure S3) and determined a cmc for SDS at 3.4 mM Figure 1, cmc labeled widi a plain bracket
    • L min-1, directly after the neutral marker (DMF) peak (Figure la,d, ). We bserved the same peak under similar conditions when only DMF was injected (see Supporting Information, Figures S3a and S8). We hypothesize that this signal arises from the partitioning of an impurity within SDS micelles (Figure 1, cmc labeled with a dotted bracket). To verify this hypothesis, we analyzed injections of a UV-absorbent hydrophobic marker into the buffer (20 μM of 2-hydroxymethyl-enenaphthalene, Figure S3) and determined a cmc for SDS at 3.4 mM (Figure 1, cmc labeled widi a plain bracket).
  • 47
    • 84869574815 scopus 로고    scopus 로고
    • th rung).
    • th rung).
  • 48
    • 84869573495 scopus 로고    scopus 로고
    • 2 are UBI-SDS∼11).
    • 2 are UBI-SDS∼11).
  • 50
    • 67849086116 scopus 로고    scopus 로고
    • The integration was performed with respect to the migration time; details available in the Supporting Information
    • The integration was performed with respect to the migration time; details available in the Supporting Information.
  • 51
    • 67849105779 scopus 로고    scopus 로고
    • The number of SDS molecules expected to bind UBI in D is 42, based on the approximation that 1 g of protein associates with 1.4 g of SDS.
    • The number of SDS molecules expected to bind UBI in D is 42, based on the approximation that 1 g of protein associates with 1.4 g of SDS.

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.