메뉴 건너뛰기




Volumn 1838, Issue 9, 2014, Pages 2289-2295

Measuring membrane penetration with depth-dependent fluorescence quenching: Distribution analysis is coming of age

Author keywords

Distribution analysis; Fluorescence quenching; Membrane penetration; Molecular dynamics simulation; Parallax method

Indexed keywords

1 PALMITOYL 2 STEAROYL GLYCERO 3 PHOSPHOCHOLINE; 2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; GLYCOPROTEIN GP 41; HYBRID PROTEIN; MEMBRANE PROTEIN; PHOSPHORYLCHOLINE; UNCLASSIFIED DRUG;

EID: 84903703964     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2014.02.019     Document Type: Review
Times cited : (38)

References (32)
  • 1
    • 0344270184 scopus 로고
    • Distribution analysis of membrane penetration by depth dependent fluorescence quenching
    • A.S. Ladokhin Distribution analysis of membrane penetration by depth dependent fluorescence quenching Biophys. J. 64 1993 A290 A
    • (1993) Biophys. J. , vol.64
    • Ladokhin, A.S.1
  • 2
    • 0031005647 scopus 로고    scopus 로고
    • Distribution analysis of depth-dependent fluorescence quenching in membranes: A practical guide
    • DOI 10.1016/S0076-6879(97)78024-8
    • A.S. Ladokhin Distribution analysis of depth-dependent fluorescence quenching in membranes: a practical guide Methods Enzymol. 278 1997 462 473 (Pubitemid 27229933)
    • (1997) Methods in Enzymology , vol.278 , pp. 462-473
    • Ladokhin, A.S.1
  • 3
    • 0033032331 scopus 로고    scopus 로고
    • Analysis of protein and peptide penetration into membranes by depth- dependent fluorescence quenching: Theoretical considerations
    • A.S. Ladokhin Analysis of protein and peptide penetration into membranes by depth-dependent fluorescence quenching: theoretical considerations Biophys. J. 76 1999 946 955 (Pubitemid 29264574)
    • (1999) Biophysical Journal , vol.76 , Issue.2 , pp. 946-955
    • Ladokhin, A.S.1
  • 4
    • 0032787129 scopus 로고    scopus 로고
    • Evaluation of lipid exposure of tryptophan residues in membrane peptides and proteins
    • A.S. Ladokhin Evaluation of lipid exposure of tryptophan residues in membrane peptides and proteins Anal. Biochem. 276 1999 65 71
    • (1999) Anal. Biochem. , vol.276 , pp. 65-71
    • Ladokhin, A.S.1
  • 5
    • 84877072901 scopus 로고    scopus 로고
    • Validation of depth-dependent fluorescence quenching in membranes by molecular dynamics simulation of tryptophan octyl ester in POPC bilayer
    • A. Kyrychenko, D.J. Tobias, and A.S. Ladokhin Validation of depth-dependent fluorescence quenching in membranes by molecular dynamics simulation of tryptophan octyl ester in POPC bilayer J. Phys. Chem. B 117 2013 4770 4778
    • (2013) J. Phys. Chem. B , vol.117 , pp. 4770-4778
    • Kyrychenko, A.1    Tobias, D.J.2    Ladokhin, A.S.3
  • 6
    • 0000639846 scopus 로고
    • Distribution analysis of membrane penetration of proteins by depth-dependent fluorescence quenching
    • A.S. Ladokhin, P.W. Holloway, and E.G. Kostrzhevska Distribution analysis of membrane penetration of proteins by depth-dependent fluorescence quenching J. Fluoresc. 3 1993 195 197
    • (1993) J. Fluoresc. , vol.3 , pp. 195-197
    • Ladokhin, A.S.1    Holloway, P.W.2    Kostrzhevska, E.G.3
  • 7
    • 0029131630 scopus 로고
    • Fluorescence of membrane-bound tryptophan octyl ester: A model for studying intrinsic fluorescence of protein-membrane interactions
    • A.S. Ladokhin, and P.W. Holloway Fluorescence of membrane-bound tryptophan octyl ester: a model for studying intrinsic fluorescence of protein-membrane interactions Biophys. J. 69 1995 506 517
    • (1995) Biophys. J. , vol.69 , pp. 506-517
    • Ladokhin, A.S.1    Holloway, P.W.2
  • 8
    • 0029258473 scopus 로고
    • Fluorescence quenching study of melittin-membrane interactions
    • A.S. Ladokhin, and P.W. Holloway Fluorescence quenching study of melittin-membrane interactions Ukr. Biochem. J. 67 1995 34 40
    • (1995) Ukr. Biochem. J. , vol.67 , pp. 34-40
    • Ladokhin, A.S.1    Holloway, P.W.2
  • 10
    • 0033586718 scopus 로고    scopus 로고
    • Time-resolved distance determination by tryptophan fluorescence quenching: Probing intermediates in membrane protein folding
    • J.H. Kleinschmidt, and L.K. Tamm Time-resolved distance determination by tryptophan fluorescence quenching: probing intermediates in membrane protein folding Biochemistry 38 1999 4996 5005
    • (1999) Biochemistry , vol.38 , pp. 4996-5005
    • Kleinschmidt, J.H.1    Tamm, L.K.2
  • 11
    • 0037044318 scopus 로고    scopus 로고
    • Lipid II induces a transmembrane orientation of the pore-forming peptide lantibiotic nisin
    • H.E. van Heusden, B. de Kruijff, and E. Breukink Lipid II induces a transmembrane orientation of the pore-forming peptide lantibiotic nisin Biochemistry 41 2002 12171 12178
    • (2002) Biochemistry , vol.41 , pp. 12171-12178
    • Van Heusden, H.E.1    De Kruijff, B.2    Breukink, E.3
  • 12
    • 23844463536 scopus 로고    scopus 로고
    • Voltage-sensor activation with a tarantula toxin as cargo
    • DOI 10.1038/nature03873
    • L.R. Phillips, M. Milescu, Y. Li-Smerin, J.A. Mindell, J.I. Kim, and K.J. Swartz Voltage-sensor activation with a tarantula toxin as cargo Nature 436 2005 857 860 (Pubitemid 41160645)
    • (2005) Nature , vol.436 , Issue.7052 , pp. 857-860
    • Phillips, L.R.1    Milescu, M.2    Li-Smerin, Y.3    Mindell, J.A.4    Kim, J.I.5    Swartz, K.J.6
  • 14
    • 84887976809 scopus 로고    scopus 로고
    • Refining membrane penetration by a combination of steady-state and time-resolved depth-dependent fluorescence quenching
    • A. Kyrychenko, and A.S. Ladokhin Refining membrane penetration by a combination of steady-state and time-resolved depth-dependent fluorescence quenching Anal. Biochem. 446 2014 19 21
    • (2014) Anal. Biochem. , vol.446 , pp. 19-21
    • Kyrychenko, A.1    Ladokhin, A.S.2
  • 16
    • 0023111150 scopus 로고
    • Determination of the depth of bromine atoms in bilayers formed from bromolipid probes
    • DOI 10.1021/bi00380a042
    • T.J. McIntosh, and P.W. Holloway Determination of the depth of bromine atoms in bilayers formed from bromolipid probes Biochemistry 26 1987 1783 1788 (Pubitemid 17047651)
    • (1987) Biochemistry , vol.26 , Issue.6 , pp. 1783-1788
    • McIntosh, T.J.1    Holloway, P.W.2
  • 17
    • 0023661650 scopus 로고
    • Distance estimate of the active center of d-β-hydroxybutyrate dehydrogenase from the membrane surface
    • L.A. Dalton, J.O. McIntyre, and S. Fleischer Distance estimate of the active center of d-β-hydroxybutyrate dehydrogenase from the membrane surface Biochemistry 26 1987 2117 2130
    • (1987) Biochemistry , vol.26 , pp. 2117-2130
    • Dalton, L.A.1    McIntyre, J.O.2    Fleischer, S.3
  • 18
    • 0041320842 scopus 로고    scopus 로고
    • The distribution of lipid attached spin probes in bilayers: Application to membrane protein topology
    • A. Vogel, H.A. Scheidt, and D. Huster The distribution of lipid attached spin probes in bilayers: application to membrane protein topology Biophys. J. 85 2003 1691 1701 (Pubitemid 37052252)
    • (2003) Biophysical Journal , vol.85 , Issue.3 , pp. 1691-1701
    • Vogel, A.1    Scheidt, H.A.2    Huster, D.3
  • 20
    • 35448961949 scopus 로고    scopus 로고
    • Methods and applications of site-directed spin labeling EPR spectroscopy
    • C.S. Klug, and J.B. Feix Methods and applications of site-directed spin labeling EPR spectroscopy Methods Cell Biol. 84 2008 617 658
    • (2008) Methods Cell Biol. , vol.84 , pp. 617-658
    • Klug, C.S.1    Feix, J.B.2
  • 21
    • 70149088976 scopus 로고    scopus 로고
    • A solution NMR approach to the measurement of amphiphile immersion depth and orientation in membrane model systems
    • M.S. Al-Abdul-Wahid, C. Neale, R. Pomes, and R.S. Prosser A solution NMR approach to the measurement of amphiphile immersion depth and orientation in membrane model systems J. Am. Chem. Soc. 131 2009 6452 6459
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 6452-6459
    • Al-Abdul-Wahid, M.S.1    Neale, C.2    Pomes, R.3    Prosser, R.S.4
  • 22
    • 77957964107 scopus 로고    scopus 로고
    • Solid-state NMR paramagnetic relaxation enhancement immersion depth studies in phospholipid bilayers
    • S. Chu, S. Maltsev, A.H. Emwas, and G.A. Lorigan Solid-state NMR paramagnetic relaxation enhancement immersion depth studies in phospholipid bilayers J. Magn. Reson. 207 2010 89 94
    • (2010) J. Magn. Reson. , vol.207 , pp. 89-94
    • Chu, S.1    Maltsev, S.2    Emwas, A.H.3    Lorigan, G.A.4
  • 23
    • 84878034660 scopus 로고    scopus 로고
    • Molecular dynamics simulations of depth distribution of spin-labeled phospholipids within lipid bilayer
    • A. Kyrychenko, and A.S. Ladokhin Molecular dynamics simulations of depth distribution of spin-labeled phospholipids within lipid bilayer J. Phys. Chem. B 117 2013 5875 5885
    • (2013) J. Phys. Chem. B , vol.117 , pp. 5875-5885
    • Kyrychenko, A.1    Ladokhin, A.S.2
  • 24
    • 35848955007 scopus 로고    scopus 로고
    • Measuring the depth of amino acid residues in membrane-inserted peptides by fluorescence quenching
    • E. London, and A.S. Ladokhin Measuring the depth of amino acid residues in membrane-inserted peptides by fluorescence quenching Curr. Top. Membr. 52 2002 89 115
    • (2002) Curr. Top. Membr. , vol.52 , pp. 89-115
    • London, E.1    Ladokhin, A.S.2
  • 25
    • 0025819980 scopus 로고
    • Transbilayer distribution of bromine in fluid bilayers containing a specifically brominated analog of dioleoylphosphatidylcholine
    • M.C. Wiener, and S.H. White Transbilayer distribution of bromine in fluid bilayers containing a specifically brominated analog of dioleoylphosphatidylcholine Biochemistry 30 1991 6997 7008
    • (1991) Biochemistry , vol.30 , pp. 6997-7008
    • Wiener, M.C.1    White, S.H.2
  • 26
    • 0023652259 scopus 로고
    • Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids
    • A. Chattopadhyay, and E. London Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids Biochemistry 26 1987 39 45
    • (1987) Biochemistry , vol.26 , pp. 39-45
    • Chattopadhyay, A.1    London, E.2
  • 27
    • 0027374437 scopus 로고
    • Extension of the parallax analysis of membrane penetration depth to the polar region of model membranes: Use of fluorescence quenching by a spin- label attached to the phospholipid polar headgroup
    • DOI 10.1021/bi00091a038
    • F.S. Abrams, and E. London Extension of the parallax analysis of membrane penetration depth to the polar region of model membranes: use of fluorescence quenching by a spin-label attached to the phospholipid polar headgroup Biochemistry 32 1993 10826 10831 (Pubitemid 23327820)
    • (1993) Biochemistry , vol.32 , Issue.40 , pp. 10826-10831
    • Abrams, F.S.1    London, E.2
  • 29
    • 84871288652 scopus 로고    scopus 로고
    • C-terminal tail of human immunodeficiency virus gp41: Functionally rich and structurally enigmatic
    • J.D. Steckbeck, A.S. Kuhlmann, and R.C. Montelaro C-terminal tail of human immunodeficiency virus gp41: functionally rich and structurally enigmatic J. Gen. Virol. 94 2013 1 19
    • (2013) J. Gen. Virol. , vol.94 , pp. 1-19
    • Steckbeck, J.D.1    Kuhlmann, A.S.2    Montelaro, R.C.3
  • 30
    • 29144463608 scopus 로고    scopus 로고
    • Lifetime fluorescence method for determining membrane topology of proteins
    • DOI 10.1016/j.ab.2005.10.023, PII S0003269705007591
    • Y.O. Posokhov, and A.S. Ladokhin Lifetime fluorescence method for determining membrane topology of proteins Anal. Biochem. 348 2006 87 93 (Pubitemid 41796461)
    • (2006) Analytical Biochemistry , vol.348 , Issue.1 , pp. 87-93
    • Posokhov, Y.O.1    Ladokhin, A.S.2
  • 31
    • 0037137178 scopus 로고    scopus 로고
    • Determining the membrane topology of proteins: Insertion pathway of a transmembrane helix of annexin 12
    • DOI 10.1021/bi0264418
    • A.S. Ladokhin, J.M. Isas, H.T. Haigler, and S.H. White Determining the membrane topology of proteins: insertion pathway of a transmembrane helix of annexin 12 Biochemistry 41 2002 13617 13626 (Pubitemid 35332698)
    • (2002) Biochemistry , vol.41 , Issue.46 , pp. 13617-13626
    • Ladokhin, A.S.1    Isas, J.M.2    Haigler, H.T.3    White, S.H.4
  • 32
    • 68849090174 scopus 로고    scopus 로고
    • Kinetic intermediate reveals staggered pH-dependent transitions along the membrane insertion pathway of the diphtheria toxin T-domain
    • A. Kyrychenko, Y.O. Posokhov, M.V. Rodnin, and A.S. Ladokhin Kinetic intermediate reveals staggered pH-dependent transitions along the membrane insertion pathway of the diphtheria toxin T-domain Biochemistry 48 2009 7584 7594
    • (2009) Biochemistry , vol.48 , pp. 7584-7594
    • Kyrychenko, A.1    Posokhov, Y.O.2    Rodnin, M.V.3    Ladokhin, A.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.