메뉴 건너뛰기




Volumn 39, Issue 4, 2010, Pages 647-656

Profiling of dynamics in protein-lipid-water systems: A time-resolved fluorescence study of a model membrane protein with the label BADAN at specific membrane depths

Author keywords

Dynamic stokes shift; Membrane polarity; Membrane bound water; Membrane embedded M13 coat protein; Solvent relaxation; Streak camera picosecond fluorescence

Indexed keywords

2 NAPHTHYLAMINE; 6 BROMOACETYL 2 DIMETHYLAMINONAPHTHALENE; 6-BROMOACETYL-2-DIMETHYLAMINONAPHTHALENE; DRUG DERIVATIVE; FLUORESCENT DYE; MEMBRANE PROTEIN; SOLVENT;

EID: 77952090002     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-009-0538-6     Document Type: Article
Times cited : (14)

References (43)
  • 1
    • 34547551083 scopus 로고    scopus 로고
    • Measurement of solvation responses at multiple sites in a globular protein
    • DOI 10.1021/jp0709104
    • P Abbyad X Shi W Childs TB McAnaney BE Cohen SG Boxer 2007 Measurement of solvation responses at multiple sites in a globular protein J Phys Chem B 111 8269 8276 10.1021/jp0709104 1:CAS:528:DC%2BD2sXmvVGltro%3D 17592867 (Pubitemid 47184403)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.28 , pp. 8269-8276
    • Abbyad, P.1    Shi, X.2    Childs, W.3    McAnaney, T.B.4    Cohen, B.E.5    Boxer, S.G.6
  • 3
    • 0000001791 scopus 로고
    • Some remarks on the interpretation of the spectral properties of prodan
    • 10.1016/0009-2614(88)87067-2 1:CAS:528:DyaL1cXhtVegurs%3D
    • A Balter W Nowak W Pawelkiewicz A Kowalczyk 1988 Some remarks on the interpretation of the spectral properties of prodan Chem Phys Lett 143 565 570 10.1016/0009-2614(88)87067-2 1:CAS:528:DyaL1cXhtVegurs%3D
    • (1988) Chem Phys Lett , vol.143 , pp. 565-570
    • Balter, A.1    Nowak, W.2    Pawelkiewicz, W.3    Kowalczyk, A.4
  • 4
    • 0022424046 scopus 로고
    • Depth-dependent flourescent quenching in micelles and membranes
    • 1:CAS:528:DyaL2MXksFSmurs%3D 3890948
    • E Blatt WH Sawyer 1985 Depth-dependent flourescent quenching in micelles and membranes Biochim Biophys Acta 822 43 62 1:CAS:528:DyaL2MXksFSmurs%3D 3890948
    • (1985) Biochim Biophys Acta , vol.822 , pp. 43-62
    • Blatt, E.1    Sawyer, W.H.2
  • 5
    • 0029850169 scopus 로고    scopus 로고
    • Log-normal description of fluorescence spectra of organic fluorophores
    • 10.1111/j.1751-1097.1996.tb02464.x 1:CAS:528:DyaK28XltVKrurw%3D
    • EA Burstein VI Emelyanenko 1996 Log-normal description of fluorescence spectra of organic fluorophores Photochem Photobiol 64 316 320 10.1111/j.1751-1097.1996.tb02464.x 1:CAS:528:DyaK28XltVKrurw%3D
    • (1996) Photochem Photobiol , vol.64 , pp. 316-320
    • Burstein, E.A.1    Emelyanenko, V.I.2
  • 6
    • 0029274213 scopus 로고
    • Measurements of the solute dependence of solvation dynamics in 1-propanol: The role of specific hydrogen-bonding interactions
    • 10.1021/j100013a060 1:CAS:528:DyaK2MXksVymsbk%3D
    • CF Chapman RS Fee M Maroncelli 1995 Measurements of the solute dependence of solvation dynamics in 1-propanol: the role of specific hydrogen-bonding interactions J Phys Chem 99 4811 4819 10.1021/j100013a060 1:CAS:528: DyaK2MXksVymsbk%3D
    • (1995) J Phys Chem , vol.99 , pp. 4811-4819
    • Chapman, C.F.1    Fee, R.S.2    Maroncelli, M.3
  • 9
    • 0032869384 scopus 로고    scopus 로고
    • Fluorescent probes used to monitor membrane interfacial polarity
    • DOI 10.1016/S0009-3084(99)00055-9, PII S0009308499000559
    • RM Epand R Kraayenhof 1999 Fluorescent probes used to monitor membrane interfacial polarity Chem Phys Lipids 101 57 64 10.1016/S0009-3084(99)00055-9 1:CAS:528:DyaK1MXltlCktb4%3D 10810925 (Pubitemid 29385551)
    • (1999) Chemistry and Physics of Lipids , vol.101 , Issue.1 , pp. 57-64
    • Epand, R.M.1    Kraayenhof, R.2
  • 13
    • 44649148267 scopus 로고    scopus 로고
    • Down to atomic-scale intracellular water dynamics
    • DOI 10.1038/embor.2008.50, PII EMBOR200850
    • M Jasnin M Moulin M Haertlein G Zaccai M Tehei 2008 Down to atomic-scale intracellular water dynamics EMBO Rep 9 543 547 10.1038/embor.2008.50 18451876 (Pubitemid 351772917)
    • (2008) EMBO Reports , vol.9 , Issue.6 , pp. 543-547
    • Jasnin, M.1    Moulin, M.2    Haertlein, M.3    Zaccai, G.4    Tehei, M.5
  • 14
    • 28544442010 scopus 로고    scopus 로고
    • Effect of hydrogen bonding on the intramolecular charge transfer fluorescence of 6-dodecanoyl-2-dimethylaminonaphtalene
    • DOI 10.1016/j.chemphys.2005.06.021, PII S0301010405002533
    • M Józefowicz KA Kozyra JR Heldt J Heldt 2005 Effect of hydrogen bonding on the intramolecular charge transfer fluorescence of 6-dodecanoyl-2-dimethylaminonaphtalene Chem Phys 320 45 53 10.1016/j.chemphys. 2005.06.021 (Pubitemid 41745244)
    • (2005) Chemical Physics , vol.320 , Issue.1 , pp. 45-53
    • Jozefowicz, M.1    Kozyra, K.A.2    Heldt, J.R.3    Heldt, J.4
  • 15
    • 33750347409 scopus 로고    scopus 로고
    • Headgroup hydration and mobility of DOTAP/DOPC bilayers: A fluorescence solvent relaxation study
    • DOI 10.1021/la061597k
    • P Jurkiewicz A Olzyńska M Langner M Hof 2006 Headgroup hydration and mobility of DOTAP/DOPC bilayers: a fluorescence solvent relaxation study Langmuir 22 8741 8749 10.1021/la061597k 1:CAS:528:DC%2BD28XpsFajtrY%3D 17014112 (Pubitemid 44626133)
    • (2006) Langmuir , vol.22 , Issue.21 , pp. 8741-8749
    • Jurkiewicz, P.1    Olzynska, A.2    Langner, M.3    Hof, M.4
  • 16
    • 4644251757 scopus 로고    scopus 로고
    • Simultaneous probing of hydration and polarity of lipid bilayers with 3-hydroxyflavone fluorescent dyes
    • DOI 10.1016/j.bbamem.2004.06.004, PII S000527360400152X
    • AS Klymchenko Y Mély AP Demchenko G Duportail 2004 Simultaneous probing of hydration and polarity of lipid bilayers with 3-hydroxyflavone fluorescent dyes Biochim Biophys Acta 1665 6 19 10.1016/j.bbamem.2004.06.004 1:CAS:528:DC%2BD2cXotFShtrk%3D 15471566 (Pubitemid 39303565)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1665 , Issue.1-2 , pp. 6-19
    • Klymchenko, A.S.1    Mely, Y.2    Demchenko, A.P.3    Duportail, G.4
  • 17
    • 4444343863 scopus 로고    scopus 로고
    • Lipid bilayer topology of the transmembrane α-helix of M13 major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy
    • DOI 10.1529/biophysj.104.043208
    • RBM Koehorst RB Spruijt FJ Vergeldt MA Hemminga 2004 Lipid bilayer topology of the transmembrane α-helix of M13 major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy Biophys J 87 1445 1455 10.1529/biophysj.104.043208 1:CAS:528:DC%2BD2cXns1Slurs%3D 15345527 (Pubitemid 39167005)
    • (2004) Biophysical Journal , vol.87 , Issue.3 , pp. 1445-1455
    • Koehorst, R.B.M.1    Spruijt, R.B.2    Vergeldt, F.J.3    Hemminga, M.A.4
  • 18
    • 43849092664 scopus 로고    scopus 로고
    • Site-directed fluorescence labeling of a membrane protein with BADAN: Probing protein topology and local environment
    • 10.1529/biophysj.107.125807 1:CAS:528:DC%2BD1cXlsF2hur0%3D 18234831
    • RBM Koehorst RB Spruijt MA Hemminga 2008 Site-directed fluorescence labeling of a membrane protein with BADAN: probing protein topology and local environment Biophys J 94 3945 3955 10.1529/biophysj.107.125807 1:CAS:528:DC%2BD1cXlsF2hur0%3D 18234831
    • (2008) Biophys J , vol.94 , pp. 3945-3955
    • Koehorst, R.B.M.1    Spruijt, R.B.2    Hemminga, M.A.3
  • 20
    • 0348198100 scopus 로고    scopus 로고
    • Does PRODAN possess a planar or twisted charge-transfer excited state? Photophysical properties of two PRODAN derivatives
    • 10.1021/jp036013r 1:CAS:528:DC%2BD3sXptVKnt7g%3D
    • BC Lobo CJ Abelt 2003 Does PRODAN possess a planar or twisted charge-transfer excited state? Photophysical properties of two PRODAN derivatives J Phys Chem A 107 10938 10943 10.1021/jp036013r 1:CAS:528: DC%2BD3sXptVKnt7g%3D
    • (2003) J Phys Chem A , vol.107 , pp. 10938-10943
    • Lobo, B.C.1    Abelt, C.J.2
  • 21
    • 1842525751 scopus 로고    scopus 로고
    • Femtosecond studies of tryptophan solvation: Correlation function and water dynamics at lipid surfaces
    • 10.1016/j.cplett.2004.03.012 1:CAS:528:DC%2BD2cXisFOktbc%3D
    • W Lu J Kim W Qiu D Zhong 2004 Femtosecond studies of tryptophan solvation: correlation function and water dynamics at lipid surfaces Chem Phys Lett 388 120 126 10.1016/j.cplett.2004.03.012 1:CAS:528:DC%2BD2cXisFOktbc%3D
    • (2004) Chem Phys Lett , vol.388 , pp. 120-126
    • Lu, W.1    Kim, J.2    Qiu, W.3    Zhong, D.4
  • 22
    • 33846847707 scopus 로고    scopus 로고
    • FRET study of membrane proteins: Determination of the tilt and orientation of the N-terminal domain of M13 major coat protein
    • DOI 10.1529/biophysj.106.095026
    • PV Nazarov RBM Koehorst WL Vos VV Apanasovich MA Hemminga 2007 FRET study of membrane proteins: determination of the tilt and orientation of the N-terminal domain of M13 major coat protein Biophys J 92 1296 1305 10.1529/biophysj.106.095026 1:CAS:528:DC%2BD2sXhvVKqsLg%3D 17114224 (Pubitemid 46203190)
    • (2007) Biophysical Journal , vol.92 , Issue.4 , pp. 1296-1305
    • Nazarov, P.V.1    Koehorst, R.B.M.2    Vos, W.L.3    Apanasovich, V.V.4    Hemminga, M.A.5
  • 23
    • 36048931839 scopus 로고    scopus 로고
    • Influence of water clustering on the dynamics of hydration water at the surface of a lysozyme
    • DOI 10.1529/biophysj.107.108753
    • A Oleinikova N Smolin I Brovchenko 2007 Influence of water clustering on the dynamics of hydration water at the surface of a lysozyme Biophys J 93 2986 3000 10.1529/biophysj.107.108753 1:CAS:528:DC%2BD2sXht1aisLnN 17631539 (Pubitemid 350097091)
    • (2007) Biophysical Journal , vol.93 , Issue.9 , pp. 2986-3000
    • Oleinikova, A.1    Smolin, N.2    Brovchenko, I.3
  • 24
    • 0002648156 scopus 로고
    • Membrane lipid domains and dynamics as detected by Laurdan fluorescence
    • 10.1007/BF00718783 1:CAS:528:DyaK2MXlsFyitb4%3D
    • T Parasassi E Gratton 1995 Membrane lipid domains and dynamics as detected by Laurdan fluorescence J Fluoresc 5 59 69 10.1007/BF00718783 1:CAS:528:DyaK2MXlsFyitb4%3D
    • (1995) J Fluoresc , vol.5 , pp. 59-69
    • Parasassi, T.1    Gratton, E.2
  • 25
    • 0000479661 scopus 로고    scopus 로고
    • Comparative theoretical study on charge-transfer fluorescence probes: 6-propanoyl-2-(N, N-dimethylamino) naphthalene and derivatives
    • 10.1021/jp981540+ 1:CAS:528:DyaK1cXltFeisrw%3D
    • ABJ Parusel W Nowak S Grimme G Kohler 1998 Comparative theoretical study on charge-transfer fluorescence probes: 6-propanoyl-2-(N, N-dimethylamino) naphthalene and derivatives J Phys Chem A 102 7149 7156 10.1021/jp981540+ 1:CAS:528:DyaK1cXltFeisrw%3D
    • (1998) J Phys Chem A , vol.102 , pp. 7149-7156
    • Parusel, A.B.J.1    Nowak, W.2    Grimme, S.3    Kohler, G.4
  • 27
    • 25444458922 scopus 로고    scopus 로고
    • Ultrafast hydration dynamics in melittin folding and aggregation: Helix formation and tetramer self-assembly
    • DOI 10.1021/jp0511754
    • W Qiu L Zhang Y-T Kao W Lu T Li J Kim GM Sollenberger L Wang D Zhong 2005 Ultrafast hydration dynamics in melittin folding and aggregation: helix formation and tetramer self-assembly J Phys Chem B 109 16901 16910 10.1021/jp0511754 1:CAS:528:DC%2BD2MXotVSltbo%3D 16853151 (Pubitemid 41367433)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.35 , pp. 16901-16910
    • Qiu, W.1    Zhang, L.2    Kao, Y.-T.3    Lu, W.4    Li, T.5    Kim, J.6    Sollenberger, G.M.7    Wang, L.8    Zhong, D.9
  • 28
    • 33748295646 scopus 로고    scopus 로고
    • Photokinetic analysis of PRODAN and LAURDAN in large unilamellar vesicles from multivariate frequency-domain fluorescence
    • DOI 10.1021/jp036664n
    • BA Rowe SL Neal 2006 Photokinetic analysis of PRODAN and LAURDAN in large unilamellar vesicles from multivariate frequency-domain fluorescence J Phys Chem B 110 15021 15028 10.1021/jp036664n 1:CAS:528:DC%2BD28XmsFCmurs%3D 16869617 (Pubitemid 44325081)
    • (2006) Journal of Physical Chemistry B , vol.110 , Issue.30 , pp. 15021-15028
    • Rowe, B.A.1    Neal, S.L.2
  • 29
    • 38349162233 scopus 로고    scopus 로고
    • Fluorescence study of the solvation of fluorescent probes prodan and laurdan in poly(ε-caprolactone)-block-poly(ethylene oxide) vesicles in aqueous solutions with tetrahydrofurane
    • 10.1021/la702277t 1:CAS:528:DC%2BD2sXhtlGqtrbE 18044937
    • R Sachl M Stepanek K Prochazka J Humpolickova M Hof 2008 Fluorescence study of the solvation of fluorescent probes prodan and laurdan in poly(ε-caprolactone)-block-poly(ethylene oxide) vesicles in aqueous solutions with tetrahydrofurane Langmuir 24 288 295 10.1021/la702277t 1:CAS:528:DC%2BD2sXhtlGqtrbE 18044937
    • (2008) Langmuir , vol.24 , pp. 288-295
    • Sachl, R.1    Stepanek, M.2    Prochazka, K.3    Humpolickova, J.4    Hof, M.5
  • 30
    • 0034299172 scopus 로고    scopus 로고
    • Excited state dipole moment of PRODAN as determined from transient dielectric loss measurements
    • 10.1021/jp0009960 1:CAS:528:DC%2BD3cXmtVOksL4%3D
    • A Samanta RW Fessenden 2000 Excited state dipole moment of PRODAN as determined from transient dielectric loss measurements J Phys Chem A 104 8972 8975 10.1021/jp0009960 1:CAS:528:DC%2BD3cXmtVOksL4%3D
    • (2000) J Phys Chem A , vol.104 , pp. 8972-8975
    • Samanta, A.1    Fessenden, R.W.2
  • 31
    • 0024468872 scopus 로고
    • Aggregation-related conformational change of the membrane-associated coat protein of bacteriophage M13
    • 10.1021/bi00449a030 1:CAS:528:DyaL1MXmtFSlurc%3D 2690954
    • RB Spruijt CJAM Wolfs MA Hemminga 1989 Aggregation-related conformational change of the membrane-associated coat protein of bacteriophage M13 Biochemistry 28 9158 9165 10.1021/bi00449a030 1:CAS:528:DyaL1MXmtFSlurc%3D 2690954
    • (1989) Biochemistry , vol.28 , pp. 9158-9165
    • Spruijt, R.B.1    Cjam, W.2    Hemminga, M.A.3
  • 32
    • 33646560648 scopus 로고    scopus 로고
    • Anchoring mechanisms of membrane-associated M13 major coat protein
    • DOI 10.1016/j.chemphyslip.2006.02.023, PII S0009308406000429
    • D Stopar RB Spruijt MA Hemminga 2006 Anchoring mechanisms of membrane-associated M13 major coat protein Chem Phys Lipids 141 83 93 10.1016/j.chemphyslip.2006.02.023 1:CAS:528:DC%2BD28XltVKntr8%3D 16620800 (Pubitemid 43728802)
    • (2006) Chemistry and Physics of Lipids , vol.141 , Issue.1-2 , pp. 83-93
    • Stopar, D.1    Spruijt, R.B.2    Hemminga, M.A.3
  • 33
    • 33751211866 scopus 로고    scopus 로고
    • Motional restrictions of membrane proteins: A site-directed spin labeling study
    • DOI 10.1529/biophysj.106.090308
    • D Stopar J Strancar RB Spruijt MA Hemminga 2006 Motional restrictions of membrane proteins: a site-directed spin labeling study Biophys J 91 3341 3348 10.1529/biophysj.106.090308 1:CAS:528:DC%2BD28XhtFensLbI 16905615 (Pubitemid 44788267)
    • (2006) Biophysical Journal , vol.91 , Issue.9 , pp. 3341-3348
    • Stopar, D.1    Strancar, J.2    Spruijt, R.B.3    Hemminga, M.A.4
  • 34
    • 34250348139 scopus 로고    scopus 로고
    • Time-dependent stokes shifts of fluorescent dyes in the hydrophobic backbone region of a phospholipid bilayer: Combination of fluorescence spectroscopy and ab initio calculations
    • DOI 10.1021/jp0719255
    • J Sýkora P Slavicek P Jungwirth J Barucha M Hof 2007 Time-dependent stokes shifts of fluorescent dyes in the hydrophobic backbone region of a phospholipid bilayer: combination of fluorescence spectroscopy and ab initio calculations J Phys Chem B 111 5869 5877 10.1021/jp0719255 17488002 (Pubitemid 46918217)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.21 , pp. 5869-5877
    • Sykora, J.1    Slavicek, P.2    Jungwirth, P.3    Barucha, J.4    Hof, M.5
  • 35
    • 59649124429 scopus 로고    scopus 로고
    • Ultrafast resonance energy transfer from a site-specifically attached fluorescent chromophore reveals the folding of the N-terminal domain of CP29
    • 10.1016/j.chemphys.2008.10.052
    • B Van Oort S Murali E Wientjes RBM Koehorst RB Spruijt A van Hoek R Croce H van Amerongen 2009 Ultrafast resonance energy transfer from a site-specifically attached fluorescent chromophore reveals the folding of the N-terminal domain of CP29 Chem Phys 357 113 119 10.1016/j.chemphys.2008.10.052
    • (2009) Chem Phys , vol.357 , pp. 113-119
    • Van Oort, B.1    Murali, S.2    Wientjes, E.3    Koehorst, R.B.M.4    Spruijt, R.B.5    Van Hoek, A.6    Croce, R.7    Van Amerongen, H.8
  • 36
    • 58649105358 scopus 로고    scopus 로고
    • (Sub)-picosecond spectral evolution of fluorescence studied with a synchroscan streak-camera system and target analysis
    • In: Aartsma TJ, Matysik J (eds) Springer, Dordrecht
    • Van Stokkum IHM, van Oort B, van Mourik F, Gobets B, van Amerongen H (2008) (Sub)-picosecond spectral evolution of fluorescence studied with a synchroscan streak-camera system and target analysis. In: Aartsma TJ, Matysik J (eds) Biophysical techniques in photosynthesis, vol 26. Springer, Dordrecht, pp 223-240
    • (2008) Biophysical Techniques in Photosynthesis , vol.26 , pp. 223-240
    • Van Stokkum, I.H.M.1    Van Oort, B.2    Van Mourik, F.3    Gobets, B.4    Van Amerongen, H.5
  • 37
    • 0030764281 scopus 로고    scopus 로고
    • Laurdan solvatochromism: Solvent dielectric relaxation and intramolecular excited-state reaction
    • 10.1016/S0006-3495(97)78253-5 1:CAS:528:DyaK2sXmsFCnurs%3D 9336218
    • M Viard J Gallay M Vincent O Meyer B Robert M Paternostre 1997 Laurdan solvatochromism: solvent dielectric relaxation and intramolecular excited-state reaction Biophys J 73 2221 2234 10.1016/S0006-3495(97)78253-5 1:CAS:528:DyaK2sXmsFCnurs%3D 9336218
    • (1997) Biophys J , vol.73 , pp. 2221-2234
    • Viard, M.1    Gallay, J.2    Vincent, M.3    Meyer, O.4    Robert, B.5    Paternostre, M.6
  • 38
    • 22244438518 scopus 로고    scopus 로고
    • Nanosecond dynamics of a mimicked membrane-water interface observed by time-resolved stokes shift of LAURDAN
    • DOI 10.1529/biophysj.104.057497
    • M Vincent B de Foresta J Gallay 2005 Nanosecond dynamics of a mimicked membrane-water interface observed by time-resolved stokes shift of LAURDAN Biophys J 88 4337 4350 10.1529/biophysj.104.057497 1:CAS:528: DC%2BD2MXksl2jtb0%3D 15778437 (Pubitemid 40991143)
    • (2005) Biophysical Journal , vol.88 , Issue.6 , pp. 4337-4350
    • Vincent, M.1    De Foresta, B.2    Gallay, J.3
  • 39
    • 33644682471 scopus 로고    scopus 로고
    • Membrane-bound conformation of M13 major coat protein: A structure validation through FRET-derived constraints
    • DOI 10.1074/jbc.M505875200
    • WL Vos RBM Koehorst RB Spruijt MA Hemminga 2005 Membrane-bound conformation of M13 major coat protein: a structure validation through FRET-derived constraints J Biol Chem 280 38522 38527 10.1074/jbc.M505875200 1:CAS:528:DC%2BD2MXht1SktLrP 16150733 (Pubitemid 43853751)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.46 , pp. 38522-38527
    • Vos, W.L.1    Koehorst, R.B.M.2    Spruijt, R.B.3    Hemminga, M.A.4
  • 40
    • 36549080549 scopus 로고    scopus 로고
    • Structure of membrane-embedded M13 major coat protein is insensitive to hydrophobic stress
    • DOI 10.1529/biophysj.107.112698
    • WL Vos M Schor PV Nazarov RBM Koehorst RB Spruijt MA Hemminga 2007 Structure of membrane-embedded M13 major coat protein is insensitive to hydrophobic stress Biophys J 93 3541 3547 10.1529/biophysj.107.112698 1:CAS:528:DC%2BD2sXht12js77M 17704180 (Pubitemid 350190816)
    • (2007) Biophysical Journal , vol.93 , Issue.10 , pp. 3541-3547
    • Vos, W.L.1    Schor, M.2    Nazarov, P.V.3    Koehorst, R.B.M.4    Spruijt, R.B.5    Hemminga, M.A.6
  • 41
    • 65549122913 scopus 로고    scopus 로고
    • From 'I' to 'L' and back again: The odyssey of membrane-bound M13 protein
    • 10.1016/j.tibs.2009.01.007 1:CAS:528:DC%2BD1MXmtVOjt78%3D 19362002
    • WL Vos PV Nazarov RBM Koehorst RB Spruijt MA Hemminga 2009 From 'I' to 'L' and back again: the odyssey of membrane-bound M13 protein Trends Biochem Sci 34 249 255 10.1016/j.tibs.2009.01.007 1:CAS:528:DC%2BD1MXmtVOjt78%3D 19362002
    • (2009) Trends Biochem Sci , vol.34 , pp. 249-255
    • Vos, W.L.1    Nazarov, P.V.2    Koehorst, R.B.M.3    Spruijt, R.B.4    Hemminga, M.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.