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Volumn 8, Issue 11, 2013, Pages 2090-2097

Quantification of free cysteines in membrane and soluble proteins using a fluorescent dye and thermal unfolding

Author keywords

[No Author keywords available]

Indexed keywords

7 DIETHYLAMINO 3 [[4' (IODOACETYL)AMINO]PHENYL] 4 METHYLCOUMARIN; CYSTEINE; DEHYDROALANINE; FLUORESCENT DYE; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 84887006416     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2013.128     Document Type: Article
Times cited : (28)

References (28)
  • 2
    • 17144391476 scopus 로고    scopus 로고
    • Identification of the hydrophobic thickness of a membrane protein using fluorescence spectroscopy: Studies with the mechanosensitive channel MscL
    • DOI 10.1021/bi047338g
    • Powl, A.M., Wright, J.N., East, J.M. & Lee, A.G. Identification of the hydrophobic thickness of a membrane protein using fluorescence spectroscopy: studies with the mechanosensitive channel MscL. Biochemistry 44, 5713-5721 (2005). (Pubitemid 40525107)
    • (2005) Biochemistry , vol.44 , Issue.15 , pp. 5713-5721
    • Powl, A.M.1    Wright, J.N.2    East, J.M.3    Lee, A.G.4
  • 3
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • Hubbell, W.L., Cafiso, D.S. & Altenbach, C. Identifying conformational changes with site-directed spin labeling. Nat. Struct. Biol. 7, 735-739 (2000).
    • (2000) Nat. Struct. Biol , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 4
    • 67649130281 scopus 로고    scopus 로고
    • Chemical modification of proteins at cysteine: Opportunities in chemistry and biology
    • Chalker, J.M., Bernardes, G.J.L., Lin, Y.A. & Davis, B.G. Chemical modification of proteins at cysteine: opportunities in chemistry and biology. Chem. Asian J. 4, 630-640 (2009).
    • (2009) Chem. Asian J , vol.4 , pp. 630-640
    • Chalker, J.M.1    Bernardes, G.J.L.2    Lin, Y.A.3    Davis, B.G.4
  • 5
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman, G.L. Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82, 70-77 (1959).
    • (1959) Arch. Biochem. Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 6
    • 0035818431 scopus 로고    scopus 로고
    • Pegylation: A method for assessing topological accessibilities in Kv 1.3
    • DOI 10.1021/bi0107647
    • Lu, J. & Deutsch, C. Pegylation: A method for assessing topological accessibilities in Kv1.3. Biochemistry 40, 13288-13301 (2001). (Pubitemid 33043545)
    • (2001) Biochemistry , vol.40 , Issue.44 , pp. 13288-13301
    • Lu, J.1    Deutsch, C.2
  • 7
    • 70350313495 scopus 로고    scopus 로고
    • Pulsed electron-electron double-resonance determination of spin-label distances and orientations on the tetrameric potassium ion channel KcsA
    • Endeward, B., Butterwick, J.A., MacKinnon, R. & Prisner, T.F. Pulsed electron-electron double-resonance determination of spin-label distances and orientations on the tetrameric potassium ion channel KcsA. J. Am. Chem. Soc. 131, 15246-15250 (2009).
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 15246-15250
    • Endeward, B.1    Butterwick, J.A.2    Mackinnon, R.3    Prisner, T.F.4
  • 8
    • 0036318194 scopus 로고    scopus 로고
    • Quick measurement of protein sulfhydryls with Ellman's reagent and with 4,4′-dithiodipyridine
    • DOI 10.1007/s00216-002-1347-2
    • Riener, C.K., Kada, G. & Gruber, H.J. Quick measurement of protein sulfhydryls with Ellman?s reagent and with 4,4?-dithiodipyridine. Anal. Bioanal. Chem. 373, 266-276 (2002). (Pubitemid 34756941)
    • (2002) Analytical and Bioanalytical Chemistry , vol.373 , Issue.4-5 , pp. 266-276
    • Riener, C.K.1    Kada, G.2    Gruber, H.J.3
  • 10
    • 77949318714 scopus 로고    scopus 로고
    • Tryptophan in the pore of the mechanosensitive channel MscS
    • Rasmussen, T. et al. Tryptophan in the pore of the mechanosensitive channel MscS. J. Biol. Chem. 285, 5377-5384 (2010).
    • (2010) J. Biol. Chem , vol.285 , pp. 5377-5384
    • Rasmussen, T.1
  • 11
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • DOI 10.1016/j.ab.2006.07.027, PII S0003269706005355
    • Ericsson, U.B., Hallberg, B.M., Detitta, G.T., Dekker, N. & Nordlund, P. Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal. Biochem. 357, 289-298 (2006). (Pubitemid 44430091)
    • (2006) Analytical Biochemistry , vol.357 , Issue.2 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    DeTitta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 12
    • 40049099087 scopus 로고    scopus 로고
    • Microscale fluorescent thermal stability assay for membrane proteins
    • DOI 10.1016/j.str.2008.02.004, PII S0969212608000609
    • Alexandrov, A.I., Mileni, M., Chien, E.Y.T., Hanson, M.A. & Stevens, R.C. Microscale fluorescent thermal stability assay for membrane proteins. Structure 16, 351-359 (2008). (Pubitemid 351324124)
    • (2008) Structure , vol.16 , Issue.3 , pp. 351-359
    • Alexandrov, A.I.1    Mileni, M.2    Chien, E.Y.T.3    Hanson, M.A.4    Stevens, R.C.5
  • 13
    • 0033534145 scopus 로고    scopus 로고
    • Determination of protein secondary structure and solvent accessibility using site-directed fluorescence labeling. Studies of T4 lysozyme using the fluorescent probe monobromobimane
    • Mansoor, S.E., Mchaourab, H.S. & Farrens, D.L. Determination of protein secondary structure and solvent accessibility using site-directed fluorescence labeling. studies of T4 lysozyme using the fluorescent probe monobromobimane. Biochemistry 38, 16383-16393 (1999). (Pubitemid 129520562)
    • (1999) Biochemistry , vol.38 , Issue.49 , pp. 16383-16393
    • Mansoor, S.E.1    McHaourab, H.S.2    Farrens, D.L.3
  • 14
    • 77951645706 scopus 로고    scopus 로고
    • LCP-Tm: An assay to measure and understand stability of membrane proteins in a membrane environment
    • Liu, W., Hanson, M.A., Stevens, R.C. & Cherezov, V. LCP-Tm: An assay to measure and understand stability of membrane proteins in a membrane environment. Biophys. J. 98, 1539-1548 (2010).
    • (2010) Biophys. J , vol.98 , pp. 1539-1548
    • Liu, W.1    Hanson, M.A.2    Stevens, R.C.3    Cherezov, V.4
  • 15
    • 0019464274 scopus 로고
    • New fluorochromes for thiols: Maleimide and iodoacetamide derivatives of a 3-phenylcoumarin fluorophore
    • Sippel, T.O. New fluorochromes for thiols: maleimide and iodoacetamide derivatives of a 3-phenylcoumarin fluorophore. J. Histochem. Cytochem. 29, 314-316 (1981). (Pubitemid 11145685)
    • (1981) Journal of Histochemistry and Cytochemistry , vol.29 , Issue.2 , pp. 314-316
    • Sippel, T.O.1
  • 16
    • 84856887479 scopus 로고    scopus 로고
    • Conversion of cysteine into dehydroalanine enables access to synthetic histones bearing diverse post-translational modifications
    • Chalker, J.M., Lercher, L., Rose, N.R., Schofield, C.J. & Davis, B.G. Conversion of cysteine into dehydroalanine enables access to synthetic histones bearing diverse post-translational modifications. Angew. Chem. 51, 1835-1839 (2012).
    • (2012) Angew. Chem , vol.51 , pp. 1835-1839
    • Chalker, J.M.1    Lercher, L.2    Rose, N.R.3    Schofield, C.J.4    Davis, B.G.5
  • 17
    • 84867067614 scopus 로고    scopus 로고
    • Conformational state of the MscS mechanosensitive channel in solution revealed by pulsed electron-electron double resonance (PELDOR) spectroscopy
    • Pliotas, C. et al. Conformational state of the MscS mechanosensitive channel in solution revealed by pulsed electron-electron double resonance (PELDOR) spectroscopy. Proc. Natl. Acad. Sci. USA 109, 2675-2682 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 2675-2682
    • Pliotas, C.1
  • 18
    • 70349777756 scopus 로고    scopus 로고
    • PELDOR spectroscopy distance fingerprinting of the octameric outer-membrane protein Wza from Escherichia coli
    • Hagelueken, G. et al. PELDOR spectroscopy distance fingerprinting of the octameric outer-membrane protein Wza from Escherichia coli. Angew. Chem. 48, 2904-2906 (2009).
    • (2009) Angew. Chem , vol.48 , pp. 2904-2906
    • Hagelueken, G.1
  • 20
    • 34250841296 scopus 로고    scopus 로고
    • Measuring distances by pulsed dipolar ESR spectroscopy: Spin-labeled histidine kinases
    • DOI 10.1016/S0076-6879(07)23003-4, PII S0076687907230034, Two Component Signaling Systems, Part B
    • Borbat, P.P. & Freed, J.H. Measuring distances by pulsed dipolar ESR spectroscopy: spin-labeled histidine kinases. Methods Enzymol. 423, 52-116 (2007). (Pubitemid 46991091)
    • (2007) Methods in Enzymology , vol.423 , pp. 52-116
    • Borbat, P.P.1    Freed, J.H.2
  • 21
    • 84859741866 scopus 로고    scopus 로고
    • Site-directed spin labeling of membrane proteins
    • Bordignon, E. Site-directed spin labeling of membrane proteins. Top. Curr. Chem. 321, 121-157 (2012).
    • (2012) Top. Curr. Chem , vol.321 , pp. 121-157
    • Bordignon, E.1
  • 22
    • 34548317408 scopus 로고    scopus 로고
    • Long-range distance determinations in biomacromolecules by EPR spectroscopy
    • DOI 10.1017/S003358350700460X
    • Schiemann, O. & Prisner, T.F. Long-range distance determinations in biomacromolecules by EPR spectroscopy. Q. Rev. Biophys. 40, 1-53 (2007). (Pubitemid 47343581)
    • (2007) Quarterly Reviews of Biophysics , vol.40 , Issue.1 , pp. 1-53
    • Schiemann, O.1    Prisner, T.F.2
  • 23
    • 81355138529 scopus 로고    scopus 로고
    • Methods for converting cysteine to dehydroalanine on peptides and proteins
    • Chalker, J.M. et al. Methods for converting cysteine to dehydroalanine on peptides and proteins. Chem. Sci. 2, 1666-1676 (2011).
    • (2011) Chem. Sci , vol.2 , pp. 1666-1676
    • Chalker, J.M.1
  • 24
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • DOI 10.1038/nature01511
    • Aebersold, R. & Mann, M. Mass spectrometry-based proteomics. Nature 422, 198-207 (2003). (Pubitemid 36362757)
    • (2003) Nature , vol.422 , Issue.6928 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 25
    • 77449160010 scopus 로고    scopus 로고
    • Subunit organization in the TatA complex of the twin arginine protein translocase: A site-directed EPR spin labeling study
    • White, G.F. et al. Subunit organization in the TatA complex of the twin arginine protein translocase: A site-directed EPR spin labeling study. J. Biol. Chem. 285, 2294-2301 (2010).
    • (2010) J. Biol. Chem , vol.285 , pp. 2294-2301
    • White, G.F.1
  • 26
    • 84864679402 scopus 로고    scopus 로고
    • Double electron-electron resonance shows cytochrome P450cam undergoes a conformational change in solution upon binding substrate
    • Stoll, S. et al. Double electron-electron resonance shows cytochrome P450cam undergoes a conformational change in solution upon binding substrate. Proc. Natl. Acad. Sci. USA 109, 12888-12893 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 12888-12893
    • Stoll, S.1
  • 27
    • 34250214534 scopus 로고    scopus 로고
    • An optimized purification and reconstitution method for the MscS channel: Strategies for spectroscopical analysis
    • DOI 10.1021/bi700322k
    • Vasquez, V., Cortes, M.D., Furukawa, H. & Perozo, E. An optimized purification and reconstitution method for the MscS channel: strategies for spectroscopical analysis. Biochemistry 46, 6766-6773 (2007). (Pubitemid 46906406)
    • (2007) Biochemistry , vol.46 , Issue.23 , pp. 6766-6773
    • Vasquez, V.1    Cortes, D.M.2    Furukawa, H.3    Perozo, E.4
  • 28
    • 80052442072 scopus 로고    scopus 로고
    • Mechanism of ubiquitylation by dimeric RING ligase RNF4
    • Plechanovová, A. et al. Mechanism of ubiquitylation by dimeric RING ligase RNF4. Nat. Struct. Mol. Biol. 18, 1052-1060 (2011).
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 1052-1060
    • Plechanovová, A.1


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