메뉴 건너뛰기




Volumn 1798, Issue 2, 2010, Pages 150-160

A method for solution NMR structural studies of large integral membrane proteins: Reverse micelle encapsulation

Author keywords

Detergents; Membrane proteins; NMR; Potassium channel; Reverse micelles; Surfactants

Indexed keywords

DETERGENT; MEMBRANE PROTEIN; POTASSIUM CHANNEL; POTASSIUM CHANNEL KCSA; SURFACTANT; UNCLASSIFIED DRUG;

EID: 74549167295     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2009.07.027     Document Type: Review
Times cited : (31)

References (44)
  • 1
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin K., Riek R., Wider G., and Wuthrich K. Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 12366-12371
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wuthrich, K.4
  • 2
    • 0032430418 scopus 로고    scopus 로고
    • High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids
    • Wand A.J., Ehrhardt M.R., and Flynn P.F. High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 15299-15302
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 15299-15302
    • Wand, A.J.1    Ehrhardt, M.R.2    Flynn, P.F.3
  • 4
    • 1842473098 scopus 로고    scopus 로고
    • Direct access to the cooperative substructure of proteins and the protein ensemble via cold denaturation
    • Babu C.R., Hilser V.J., and Wand A.J. Direct access to the cooperative substructure of proteins and the protein ensemble via cold denaturation. Nat. Struct. Mol. Biol. 11 (2004) 352-357
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 352-357
    • Babu, C.R.1    Hilser, V.J.2    Wand, A.J.3
  • 5
    • 3543054174 scopus 로고    scopus 로고
    • Forced folding and structural analysis of metastable proteins
    • Peterson R.W., Anbalagan K., Tommos C., and Wand A.J. Forced folding and structural analysis of metastable proteins. J. Am. Chem. Soc. 126 (2004) 9498-9499
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 9498-9499
    • Peterson, R.W.1    Anbalagan, K.2    Tommos, C.3    Wand, A.J.4
  • 6
    • 61449167023 scopus 로고    scopus 로고
    • Reverse micelles in integral membrane protein structural biology by solution NMR spectroscopy
    • Kielec J.M., Valentine K.G., and Wand A.J. Reverse micelles in integral membrane protein structural biology by solution NMR spectroscopy. Structure 17 (2009) 345-351
    • (2009) Structure , vol.17 , pp. 345-351
    • Kielec, J.M.1    Valentine, K.G.2    Wand, A.J.3
  • 7
    • 41149160641 scopus 로고    scopus 로고
    • Use of reverse micelles in membrane protein structural biology
    • Van Horn W.D., Ogilvie M.E., and Flynn P.F. Use of reverse micelles in membrane protein structural biology. J. Biomol. NMR 40 (2008) 203-211
    • (2008) J. Biomol. NMR , vol.40 , pp. 203-211
    • Van Horn, W.D.1    Ogilvie, M.E.2    Flynn, P.F.3
  • 8
    • 25844460047 scopus 로고    scopus 로고
    • Self contained high pressure cell, apparatus and procedure for the preparation of encapsulated proteins dissolved in low viscosity fluids for NMR spectroscopy
    • Peterson R.W., and Wand A.J. Self contained high pressure cell, apparatus and procedure for the preparation of encapsulated proteins dissolved in low viscosity fluids for NMR spectroscopy. Rev. Sci. Instrum. 76 (2005) 1-7
    • (2005) Rev. Sci. Instrum. , vol.76 , pp. 1-7
    • Peterson, R.W.1    Wand, A.J.2
  • 9
    • 22944431904 scopus 로고    scopus 로고
    • High-resolution NMR studies of encapsulated proteins in liquid ethane
    • Peterson R.W., Lefebvre B.G., and Wand A.J. High-resolution NMR studies of encapsulated proteins in liquid ethane. J. Am. Chem. Soc. 127 (2005) 10176-10177
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 10176-10177
    • Peterson, R.W.1    Lefebvre, B.G.2    Wand, A.J.3
  • 10
    • 33645504750 scopus 로고    scopus 로고
    • NMR study of the tetrameric KcsA potassium channel in detergent micelles
    • Chill J.H., Louis J.M., Miller C., and Bax A. NMR study of the tetrameric KcsA potassium channel in detergent micelles. Protein Sci. 15 (2006) 684-698
    • (2006) Protein Sci. , vol.15 , pp. 684-698
    • Chill, J.H.1    Louis, J.M.2    Miller, C.3    Bax, A.4
  • 11
    • 0034923122 scopus 로고    scopus 로고
    • High-resolution nuclear magnetic resonance of encapsulated proteins dissolved in low viscosity fluids
    • Flynn P.F., and Wand A.J. High-resolution nuclear magnetic resonance of encapsulated proteins dissolved in low viscosity fluids. Nucl. Magn. Reson. Biol. Macromol. Pt B 339 (2001) 54-70
    • (2001) Nucl. Magn. Reson. Biol. Macromol. Pt B , vol.339 , pp. 54-70
    • Flynn, P.F.1    Wand, A.J.2
  • 12
    • 4043161956 scopus 로고    scopus 로고
    • Multidimensional multinuclear solution NMR studies of encapsulated macromolecules
    • Flynn P.F. Multidimensional multinuclear solution NMR studies of encapsulated macromolecules. Prog. NMR Spectrosc. 45 (2004) 31-51
    • (2004) Prog. NMR Spectrosc. , vol.45 , pp. 31-51
    • Flynn, P.F.1
  • 13
    • 0014504023 scopus 로고
    • The cetyltrimethylammonium bromide-hexanol-water system
    • Ekwall P., Mandell L., and Fontell K. The cetyltrimethylammonium bromide-hexanol-water system. J. Colloid Interface Sci. 29 (1969) 639-646
    • (1969) J. Colloid Interface Sci. , vol.29 , pp. 639-646
    • Ekwall, P.1    Mandell, L.2    Fontell, K.3
  • 14
    • 28044436290 scopus 로고    scopus 로고
    • New reverse micelle surfactant systems optimized for high-resolution NMR Spectroscopy of encapsulated proteins
    • Shi Z.S., Peterson R.W., and Wand A.J. New reverse micelle surfactant systems optimized for high-resolution NMR Spectroscopy of encapsulated proteins. Langmuir 21 (2005) 10632-10637
    • (2005) Langmuir , vol.21 , pp. 10632-10637
    • Shi, Z.S.1    Peterson, R.W.2    Wand, A.J.3
  • 15
    • 19944370871 scopus 로고    scopus 로고
    • NMR spectroscopy of proteins encapsulated in a positively charged surfactant
    • Lefebvre B.G., Liu W., Peterson R.W., Valentine K.G., and Wand A.J. NMR spectroscopy of proteins encapsulated in a positively charged surfactant. J. Magn. Reson. 175 (2005) 158-162
    • (2005) J. Magn. Reson. , vol.175 , pp. 158-162
    • Lefebvre, B.G.1    Liu, W.2    Peterson, R.W.3    Valentine, K.G.4    Wand, A.J.5
  • 16
    • 27644439602 scopus 로고    scopus 로고
    • Novel surfactant mixtures for NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids
    • Peterson R.W., Pometun M.S., Shi Z., and Wand A.J. Novel surfactant mixtures for NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids. Protein Sci. 14 (2005) 2919-2921
    • (2005) Protein Sci. , vol.14 , pp. 2919-2921
    • Peterson, R.W.1    Pometun, M.S.2    Shi, Z.3    Wand, A.J.4
  • 18
    • 0034679114 scopus 로고    scopus 로고
    • Optimal use of cryogenic probe technology in NMR studies of proteins
    • Flynn P.F., Mattiello D.L., Hill H.D.W., and Wand A.J. Optimal use of cryogenic probe technology in NMR studies of proteins. J. Am. Chem. Soc. 122 (2000) 4823-4824
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 4823-4824
    • Flynn, P.F.1    Mattiello, D.L.2    Hill, H.D.W.3    Wand, A.J.4
  • 19
    • 0001147833 scopus 로고    scopus 로고
    • NMR of biomolecules in low viscosity, liquid CO2
    • Gaemers S., Elsevier C.J., and Bax A. NMR of biomolecules in low viscosity, liquid CO2. Chem. Phys. Lett. 301 (1999) 138-144
    • (1999) Chem. Phys. Lett. , vol.301 , pp. 138-144
    • Gaemers, S.1    Elsevier, C.J.2    Bax, A.3
  • 20
    • 14844362000 scopus 로고    scopus 로고
    • Reverse micelles dissolved in supercritical xenon: an NMR spectroscopic study
    • Meier M., Fink A., and Brunner E. Reverse micelles dissolved in supercritical xenon: an NMR spectroscopic study. J. Phys. Chem. B 109 (2005) 3494-3498
    • (2005) J. Phys. Chem. B , vol.109 , pp. 3494-3498
    • Meier, M.1    Fink, A.2    Brunner, E.3
  • 21
    • 0038069358 scopus 로고    scopus 로고
    • Preparation, characterization, and NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids
    • Babu C.R., Flynn P.F., and Wand A.J. Preparation, characterization, and NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids. J. Biomol. NMR 25 (2003) 313-323
    • (2003) J. Biomol. NMR , vol.25 , pp. 313-323
    • Babu, C.R.1    Flynn, P.F.2    Wand, A.J.3
  • 22
    • 0018689354 scopus 로고
    • Rhodopsin-phospholipid complexes in apolar environments: photochemical characterization
    • Darszon A., Strasser R.J., and Montal M. Rhodopsin-phospholipid complexes in apolar environments: photochemical characterization. Biochemistry 18 (1979) 5205-5213
    • (1979) Biochemistry , vol.18 , pp. 5205-5213
    • Darszon, A.1    Strasser, R.J.2    Montal, M.3
  • 23
    • 0021111893 scopus 로고
    • A small angle X-ray scattering study of a rhodopsin-lipid complex in hexane
    • Ramakrishnan V.R., Darszon A., and Montal M. A small angle X-ray scattering study of a rhodopsin-lipid complex in hexane. J. Biol. Chem. 258 (1983) 4857-4860
    • (1983) J. Biol. Chem. , vol.258 , pp. 4857-4860
    • Ramakrishnan, V.R.1    Darszon, A.2    Montal, M.3
  • 24
    • 0024673427 scopus 로고
    • Structural parameters of the myelin transmembrane proteolipid in reverse micelles
    • Binks B.P., Chatenay D., Nicot C., Urbach W., and Waks M. Structural parameters of the myelin transmembrane proteolipid in reverse micelles. Biophys. J. 55 (1989) 949-955
    • (1989) Biophys. J. , vol.55 , pp. 949-955
    • Binks, B.P.1    Chatenay, D.2    Nicot, C.3    Urbach, W.4    Waks, M.5
  • 26
    • 0037015161 scopus 로고    scopus 로고
    • Lipids in the structure, folding, and function of the KcsA K+ channel
    • Valiyaveetil F.I., Zhou Y., and MacKinnon R. Lipids in the structure, folding, and function of the KcsA K+ channel. Biochemistry 41 (2002) 10771-10777
    • (2002) Biochemistry , vol.41 , pp. 10771-10777
    • Valiyaveetil, F.I.1    Zhou, Y.2    MacKinnon, R.3
  • 28
    • 0029643523 scopus 로고
    • Proten folding intermediates - native state hydrogen exchange
    • Bai Y.W., Sosnick T.R., Mayne L., and Englander S.W. Proten folding intermediates - native state hydrogen exchange. Science 269 (1995) 192-197
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.W.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 29
    • 0032516448 scopus 로고    scopus 로고
    • Local stability and dynamics of apocytochrome b(562) examined by the dependence of hydrogen exchange on hydrostatic pressure
    • Fuentes E.J., and Wand A.J. Local stability and dynamics of apocytochrome b(562) examined by the dependence of hydrogen exchange on hydrostatic pressure. Biochemistry 37 (1998) 9877-9883
    • (1998) Biochemistry , vol.37 , pp. 9877-9883
    • Fuentes, E.J.1    Wand, A.J.2
  • 32
  • 33
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler M., Schleucher J., and Griesinger C. Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog. NMR Spectrosc. 34 (1999) 93-158
    • (1999) Prog. NMR Spectrosc. , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 34
    • 0023662538 scopus 로고
    • Main-chain directed strategy for the assignment of H1 NMR spectra of proteins
    • Englander S.W., and Wand A.J. Main-chain directed strategy for the assignment of H1 NMR spectra of proteins. Biochemistry 26 (1987) 5953-5958
    • (1987) Biochemistry , vol.26 , pp. 5953-5958
    • Englander, S.W.1    Wand, A.J.2
  • 35
    • 0023522384 scopus 로고
    • Two-dimensional H1 NMR study of human ubiquitin - a main chain directed assignment and structure analysis
    • Distefano D.L., and Wand A.J. Two-dimensional H1 NMR study of human ubiquitin - a main chain directed assignment and structure analysis. Biochemistry 26 (1987) 7272-7281
    • (1987) Biochemistry , vol.26 , pp. 7272-7281
    • Distefano, D.L.1    Wand, A.J.2
  • 36
    • 0025829776 scopus 로고
    • Refinement of the main chain directed assignment strategy for the analysis of H1 NMR spectra of proteins
    • Wand A.J., and Nelson S.J. Refinement of the main chain directed assignment strategy for the analysis of H1 NMR spectra of proteins. Biophys. J. 59 (1991) 1101-1112
    • (1991) Biophys. J. , vol.59 , pp. 1101-1112
    • Wand, A.J.1    Nelson, S.J.2
  • 37
    • 0035013633 scopus 로고    scopus 로고
    • Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating
    • Cortes D.M., Cuello L.G., and Perozo E. Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating. J. Gen. Physiol. 117 (2001) 165-180
    • (2001) J. Gen. Physiol. , vol.117 , pp. 165-180
    • Cortes, D.M.1    Cuello, L.G.2    Perozo, E.3
  • 38
    • 0034684181 scopus 로고    scopus 로고
    • Measurement of proton, nitrogen, and carbonyl chemical shielding anisotropies in a protein dissolved in a dilute liquid crystalline phase
    • Cornilescu G., and Bax A. Measurement of proton, nitrogen, and carbonyl chemical shielding anisotropies in a protein dissolved in a dilute liquid crystalline phase. J. Am. Chem. Soc. 122 (2000) 10143-10154
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 10143-10154
    • Cornilescu, G.1    Bax, A.2
  • 39
    • 0347610773 scopus 로고
    • Empirical correlation between protein backbone conformation and C.alpha. and C.beta. 13C nuclear magnetic resonance chemical shifts
    • Spera S., and Bax A. Empirical correlation between protein backbone conformation and C.alpha. and C.beta. 13C nuclear magnetic resonance chemical shifts. J. Am. Chem. Soc. 113 (1991) 5490-5492
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 40
    • 0037354231 scopus 로고
    • RefDB: a database of uniformly referenced protein chemical shifts
    • Zhang H., Neal S., and Wishart D.S. RefDB: a database of uniformly referenced protein chemical shifts. J. Biol. NMR 25 (1993) 173-195
    • (1993) J. Biol. NMR , vol.25 , pp. 173-195
    • Zhang, H.1    Neal, S.2    Wishart, D.S.3
  • 42
    • 0035499892 scopus 로고    scopus 로고
    • Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 Å resolution
    • Zhou Y., Morais-Cabral J.H., Kaufman A., and MacKinnon R. Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 Å resolution. Nature 414 (2001) 43-48
    • (2001) Nature , vol.414 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    MacKinnon, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.