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Volumn 36, Issue , 2007, Pages 233-260

Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy

Author keywords

Atomic force microscopy; Ligand binding; Protein folding; Protein unfolding; Structure function

Indexed keywords

MEMBRANE PROTEIN;

EID: 34347259478     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.36.040306.132640     Document Type: Review
Times cited : (113)

References (82)
  • 1
    • 22144455993 scopus 로고    scopus 로고
    • Abels JA, Moreno-Herrero F, der van Heijden T, Dekker C, Dekker NH. 2005. Single-molecule measurements of the persistence length of double-stranded RNA. Biophys. J. 88:2737-44
    • Abels JA, Moreno-Herrero F, der van Heijden T, Dekker C, Dekker NH. 2005. Single-molecule measurements of the persistence length of double-stranded RNA. Biophys. J. 88:2737-44
  • 2
    • 0029847652 scopus 로고    scopus 로고
    • Improved prediction for the structure of the dimeric transmembrane domain of glycophorin A obtained through global searching
    • Adams PD, Engelman DM, Brunger AT. 1996. Improved prediction for the structure of the dimeric transmembrane domain of glycophorin A obtained through global searching. Proteins 26:257-61
    • (1996) Proteins , vol.26 , pp. 257-261
    • Adams, P.D.1    Engelman, D.M.2    Brunger, A.T.3
  • 4
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB. 1973. Principles that govern the folding of protein chains. Science 181:223-30
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 5
    • 33645300737 scopus 로고    scopus 로고
    • From molecule to malady
    • Ashcroft FM. 2006. From molecule to malady. Nature 440:440-47
    • (2006) Nature , vol.440 , pp. 440-447
    • Ashcroft, F.M.1
  • 6
    • 0034734237 scopus 로고    scopus 로고
    • Unravelling the folding of bacteriorhodopsin
    • Booth PJ. 2000. Unravelling the folding of bacteriorhodopsin. Biochim. Biophys. Acta 1460:4-14
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 4-14
    • Booth, P.J.1
  • 9
    • 28444488355 scopus 로고    scopus 로고
    • Solving the membrane protein folding problem
    • Bowie JU. 2005. Solving the membrane protein folding problem. Nature 438:581-89
    • (2005) Nature , vol.438 , pp. 581-589
    • Bowie, J.U.1
  • 12
    • 11744267490 scopus 로고
    • Measuring surface forces in aqueous solution with the atomic force microscope
    • Butt HJ, Jaschke M, Ducker W. 1995. Measuring surface forces in aqueous solution with the atomic force microscope. Bioelectrochem. Bioenerg. 38:191-201
    • (1995) Bioelectrochem. Bioenerg , vol.38 , pp. 191-201
    • Butt, H.J.1    Jaschke, M.2    Ducker, W.3
  • 13
    • 3042517378 scopus 로고    scopus 로고
    • Non-native interhelical hydrogen bonds in the cystic fibrosis transmembrane conductance regulator domain modulated by polar mutations
    • Choi MY, Cardarelli L, Therien AG, Deber CM. 2004. Non-native interhelical hydrogen bonds in the cystic fibrosis transmembrane conductance regulator domain modulated by polar mutations. Biochemistry 43:8077-83
    • (2004) Biochemistry , vol.43 , pp. 8077-8083
    • Choi, M.Y.1    Cardarelli, L.2    Therien, A.G.3    Deber, C.M.4
  • 14
    • 13844298943 scopus 로고    scopus 로고
    • Probing origins of molecular interactions stabilizing the membrane proteins halorhodopsin and bacteriorhodopsin
    • Cisneros DA, Oesterhelt D, Muller DJ. 2005. Probing origins of molecular interactions stabilizing the membrane proteins halorhodopsin and bacteriorhodopsin. Structure 13:235-42
    • (2005) Structure , vol.13 , pp. 235-242
    • Cisneros, D.A.1    Oesterhelt, D.2    Muller, D.J.3
  • 15
    • 0037686252 scopus 로고    scopus 로고
    • The present view of the mechanism of protein folding
    • Daggett V, Fersht A. 2003. The present view of the mechanism of protein folding. Nat. Rev. Mol. Cell Biol. 4:497-502
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 497-502
    • Daggett, V.1    Fersht, A.2
  • 17
    • 0032993447 scopus 로고    scopus 로고
    • Polymer principles and protein folding
    • Dill KA. 1999. Polymer principles and protein folding. Protein Sci. 8:1166-80
    • (1999) Protein Sci , vol.8 , pp. 1166-1180
    • Dill, K.A.1
  • 18
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson CM. 2003. Protein folding and misfolding. Nature 426:884-90
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 19
    • 3843102625 scopus 로고    scopus 로고
    • Sequence context modulates the stability of a GxxxG-mediated transmembrane helix-helix dimer
    • Doura AK, Kobus FJ, Dubrovsky L, Hibbard E, Fleming KG. 2004. Sequence context modulates the stability of a GxxxG-mediated transmembrane helix-helix dimer. J. Mol. Biol. 341:991-98
    • (2004) J. Mol. Biol , vol.341 , pp. 991-998
    • Doura, A.K.1    Kobus, F.J.2    Dubrovsky, L.3    Hibbard, E.4    Fleming, K.G.5
  • 20
    • 0034677966 scopus 로고    scopus 로고
    • Drug discovery: A historical perspective
    • Drews J. 2000. Drug discovery: a historical perspective. Science 287:1960-64
    • (2000) Science , vol.287 , pp. 1960-1964
    • Drews, J.1
  • 21
    • 0343777458 scopus 로고    scopus 로고
    • Observing single biomolecules at work with the atomic force microscope
    • Engel A, Müller DJ. 2000. Observing single biomolecules at work with the atomic force microscope. Nat. Struct. Biol. 7:715-18
    • (2000) Nat. Struct. Biol , vol.7 , pp. 715-718
    • Engel, A.1    Müller, D.J.2
  • 24
    • 1542513548 scopus 로고    scopus 로고
    • Force-clamp spectroscopy monitors the folding trajectory of a single protein
    • Fernandez JM, Li H. 2004. Force-clamp spectroscopy monitors the folding trajectory of a single protein. Science 303:1674-78
    • (2004) Science , vol.303 , pp. 1674-1678
    • Fernandez, J.M.1    Li, H.2
  • 26
    • 0028815284 scopus 로고
    • Forces and factors that contribute to the structural stability of membrane proteins
    • Haltia T, Freire E. 1995. Forces and factors that contribute to the structural stability of membrane proteins. Biochim. Biophys. Acta 1228:1-27
    • (1995) Biochim. Biophys. Acta , vol.1228 , pp. 1-27
    • Haltia, T.1    Freire, E.2
  • 27
    • 0030723767 scopus 로고    scopus 로고
    • Spontaneous, pH-dependent membrane insertion of a transbilayer alpha-helix
    • Hunt JF, Rath P, Rothschild KJ, Engelman DM. 1997. Spontaneous, pH-dependent membrane insertion of a transbilayer alpha-helix. Biochemistry 36:15177-92
    • (1997) Biochemistry , vol.36 , pp. 15177-15192
    • Hunt, J.F.1    Rath, P.2    Rothschild, K.J.3    Engelman, D.M.4
  • 29
    • 0035942215 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants
    • Hwa J, Klein-Seetharaman J, Khorana HG. 2001. Structure and function in rhodopsin: mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants. Proc. Natl. Acad. Sci. USA 98:4872-76
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4872-4876
    • Hwa, J.1    Klein-Seetharaman, J.2    Khorana, H.G.3
  • 31
    • 0141753133 scopus 로고    scopus 로고
    • Unfolding pathways of native bacteriorhodopsin depend on temperature
    • Janovjak H, Kessler M, Gaub H, Oesterhelt D, Müller DJ. 2003. Unfolding pathways of native bacteriorhodopsin depend on temperature. EMBO J. 22:5220-29
    • (2003) EMBO J , vol.22 , pp. 5220-5229
    • Janovjak, H.1    Kessler, M.2    Gaub, H.3    Oesterhelt, D.4    Müller, D.J.5
  • 32
    • 0034665438 scopus 로고    scopus 로고
    • Force spectroscopy of molecular systems: Single molecule force spectroscopy of polymers and biomolecules
    • Janshoff A, Neitzert M, Oberdörfer Y, Fuchs H. 2000. Force spectroscopy of molecular systems: single molecule force spectroscopy of polymers and biomolecules. Angew. Chem. Int. Ed. Engl. 39:3212-37
    • (2000) Angew. Chem. Int. Ed. Engl , vol.39 , pp. 3212-3237
    • Janshoff, A.1    Neitzert, M.2    Oberdörfer, Y.3    Fuchs, H.4
  • 33
    • 0026642866 scopus 로고
    • Bacteriorhodopsin can be refolded from two independently stable transmembrane helices and the complementary five-helix fragment
    • Kahn TW, Engelmann DM. 1992. Bacteriorhodopsin can be refolded from two independently stable transmembrane helices and the complementary five-helix fragment. Biochemistry 31:6144-51
    • (1992) Biochemistry , vol.31 , pp. 6144-6151
    • Kahn, T.W.1    Engelmann, D.M.2
  • 34
    • 28844490188 scopus 로고    scopus 로고
    • Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli
    • Kedrov A, Janovjak H, Ziegler C, Kuhlbrandt W, Muller DJ. 2006. Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli. J. Mol. Biol. 355:2-8
    • (2006) J. Mol. Biol , vol.355 , pp. 2-8
    • Kedrov, A.1    Janovjak, H.2    Ziegler, C.3    Kuhlbrandt, W.4    Muller, D.J.5
  • 36
    • 3242796697 scopus 로고    scopus 로고
    • Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy
    • Kedrov A, Ziegler C, Janovjak H, Kühlbrandt W, Müller DJ. 2004. Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy. J. Mol. Biol. 340:1143-52
    • (2004) J. Mol. Biol , vol.340 , pp. 1143-1152
    • Kedrov, A.1    Ziegler, C.2    Janovjak, H.3    Kühlbrandt, W.4    Müller, D.J.5
  • 37
    • 33748467970 scopus 로고    scopus 로고
    • Differentiating ligand and inhibitor interactions ofa single antiporter
    • Kedrov A, Ziegler C, Muller DJ. 2006. Differentiating ligand and inhibitor interactions ofa single antiporter. J. Mol. Biol. 362:925-32
    • (2006) J. Mol. Biol , vol.362 , pp. 925-932
    • Kedrov, A.1    Ziegler, C.2    Muller, D.J.3
  • 38
    • 33644844356 scopus 로고    scopus 로고
    • Unfolding barriers in bacteriorhodopsin probed from the cytoplasmic and the extracellular side by AFM
    • Kessler M, Gaub HE. 2006. Unfolding barriers in bacteriorhodopsin probed from the cytoplasmic and the extracellular side by AFM. Structure 14:521-27
    • (2006) Structure , vol.14 , pp. 521-527
    • Kessler, M.1    Gaub, H.E.2
  • 40
    • 0037474445 scopus 로고    scopus 로고
    • Alpha-hairpin stability and folding of transmembrane segments
    • Khutorsky V. 2003. Alpha-hairpin stability and folding of transmembrane segments. Biochem. Biophys. Res. Commun. 301:31-34
    • (2003) Biochem. Biophys. Res. Commun , vol.301 , pp. 31-34
    • Khutorsky, V.1
  • 41
    • 15944387765 scopus 로고    scopus 로고
    • Dual role of interactions between membranous and soluble portions of helical membrane receptors for folding and signaling
    • Klein-Seetharaman J. 2005. Dual role of interactions between membranous and soluble portions of helical membrane receptors for folding and signaling. Trends Pharmacol. Sci. 26:183-89
    • (2005) Trends Pharmacol. Sci , vol.26 , pp. 183-189
    • Klein-Seetharaman, J.1
  • 42
    • 0034717007 scopus 로고    scopus 로고
    • Structure of the light-driven chloride pump halorhodopsin at 1.8 Å resolution
    • Kolbe M, Besir H, Essen LO, Oesterhelt D. 2000. Structure of the light-driven chloride pump halorhodopsin at 1.8 Å resolution. Science 288:1390-96
    • (2000) Science , vol.288 , pp. 1390-1396
    • Kolbe, M.1    Besir, H.2    Essen, L.O.3    Oesterhelt, D.4
  • 43
    • 18444364820 scopus 로고    scopus 로고
    • Automated alignment and pattern recognition of single-molecule force spectroscopy data
    • Kuhn M, Janovjak H, Hubain M, Müller DJ. 2005. Automated alignment and pattern recognition of single-molecule force spectroscopy data. J. Microsc. 218:125-32
    • (2005) J. Microsc , vol.218 , pp. 125-132
    • Kuhn, M.1    Janovjak, H.2    Hubain, M.3    Müller, D.J.4
  • 44
    • 0033613815 scopus 로고    scopus 로고
    • Folding of amphipathic alpha-helices on membranes: Energetics of helix formation by melittin
    • Ladokhin AS, White SH. 1999. Folding of amphipathic alpha-helices on membranes: energetics of helix formation by melittin. J. Mol. Biol. 285:1363-69
    • (1999) J. Mol. Biol , vol.285 , pp. 1363-1369
    • Ladokhin, A.S.1    White, S.H.2
  • 45
    • 0038010641 scopus 로고    scopus 로고
    • Position-dependence of stabilizing polar interactions of asparagine in transmembrane helical bundles
    • Lear JD, Gratkowski H, Adamian L, Liang J, DeGrado WF. 2003. Position-dependence of stabilizing polar interactions of asparagine in transmembrane helical bundles. Biochemistry 42:6400-7
    • (2003) Biochemistry , vol.42 , pp. 6400-6407
    • Lear, J.D.1    Gratkowski, H.2    Adamian, L.3    Liang, J.4    DeGrado, W.F.5
  • 46
    • 0028381539 scopus 로고
    • Sensing discrete streptavidin-biotin interactions with atomic force microscopy
    • Lee GU, Kidwell DA, Colton RJ. 1994. Sensing discrete streptavidin-biotin interactions with atomic force microscopy. Langmuir 10:354-57
    • (1994) Langmuir , vol.10 , pp. 354-357
    • Lee, G.U.1    Kidwell, D.A.2    Colton, R.J.3
  • 47
    • 33646902110 scopus 로고    scopus 로고
    • Folding and stability of alpha-helical integral membrane proteins
    • MacKenzie KR. 2006. Folding and stability of alpha-helical integral membrane proteins. Chem. Rev. 106:1931-77
    • (2006) Chem. Rev , vol.106 , pp. 1931-1977
    • MacKenzie, K.R.1
  • 48
    • 0028375446 scopus 로고
    • Bending and twisting elasticity of DNA
    • Marko JF, Siggia ED. 1994. Bending and twisting elasticity of DNA. Macromolecules 27:981-88
    • (1994) Macromolecules , vol.27 , pp. 981-988
    • Marko, J.F.1    Siggia, E.D.2
  • 50
    • 0032502747 scopus 로고    scopus 로고
    • Refolding of bacteriorhodopsin from expressed polypeptide fragments
    • Marti T. 1998. Refolding of bacteriorhodopsin from expressed polypeptide fragments. J. Biol. Chem. 273:9312-22
    • (1998) J. Biol. Chem , vol.273 , pp. 9312-9322
    • Marti, T.1
  • 51
    • 0033531109 scopus 로고    scopus 로고
    • Energy landscapes of receptor-ligand bonds explored with dynamic force microscopy
    • Merkel R, Nassoy P, Leung A, Ritchie K, Evans E. 1999. Energy landscapes of receptor-ligand bonds explored with dynamic force microscopy. Nature 397:50-53
    • (1999) Nature , vol.397 , pp. 50-53
    • Merkel, R.1    Nassoy, P.2    Leung, A.3    Ritchie, K.4    Evans, E.5
  • 52
    • 0037452868 scopus 로고    scopus 로고
    • Sequence analyses of G-protein-coupled receptors: Similarities to rhodopsin
    • Mirzadegan T, Benko G, Filipek S, Palczewski K. 2003. Sequence analyses of G-protein-coupled receptors: similarities to rhodopsin. Biochemistry 42:2759-67
    • (2003) Biochemistry , vol.42 , pp. 2759-2767
    • Mirzadegan, T.1    Benko, G.2    Filipek, S.3    Palczewski, K.4
  • 53
    • 0141595787 scopus 로고    scopus 로고
    • Tapping mode atomic force microscopy produces faithful high-resolution images of protein surfaces
    • Möller C, Allen M, Elings V, Engel A, Müller DJ. 1999. Tapping mode atomic force microscopy produces faithful high-resolution images of protein surfaces. Biophys. J. 77:1050-58
    • (1999) Biophys. J , vol.77 , pp. 1050-1058
    • Möller, C.1    Allen, M.2    Elings, V.3    Engel, A.4    Müller, D.J.5
  • 55
    • 0028140707 scopus 로고
    • Intermolecular forces and energies between ligands and receptors
    • Moy VT, Florin EL, Gaub HE. 1994. Intermolecular forces and energies between ligands and receptors. Science 266:257-59
    • (1994) Science , vol.266 , pp. 257-259
    • Moy, V.T.1    Florin, E.L.2    Gaub, H.E.3
  • 56
    • 33747872339 scopus 로고    scopus 로고
    • Analysis assistant for single-molecule force spectroscopy data on membrane proteins-MPTV
    • Mueller F, Muller DJ, Labudde D. 2006. Analysis assistant for single-molecule force spectroscopy data on membrane proteins-MPTV. Bioinformatics 22:1796-99
    • (2006) Bioinformatics , vol.22 , pp. 1796-1799
    • Mueller, F.1    Muller, D.J.2    Labudde, D.3
  • 57
    • 0031194571 scopus 로고    scopus 로고
    • Adsorption of biological molecules to a solid support for scanning probe microscopy
    • Müller DJ, Amrein M, Engel A. 1997. Adsorption of biological molecules to a solid support for scanning probe microscopy. J. Struct. Biol. 119:172-88
    • (1997) J. Struct. Biol , vol.119 , pp. 172-188
    • Müller, D.J.1    Amrein, M.2    Engel, A.3
  • 58
    • 0041841000 scopus 로고    scopus 로고
    • Mapping flexible protein domains at subnanometer resolution with the AFM
    • Müller DJ, Fotiadis D, Engel A. 1998. Mapping flexible protein domains at subnanometer resolution with the AFM. FEBS Lett. 430:105-11
    • (1998) FEBS Lett , vol.430 , pp. 105-111
    • Müller, D.J.1    Fotiadis, D.2    Engel, A.3
  • 59
    • 0039114981 scopus 로고    scopus 로고
    • Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscopy
    • Müller DJ, Fotiadis D, Scheuring S, Müller SA, Engel A. 1999. Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscopy. Biophys. J. 76:1101-11
    • (1999) Biophys. J , vol.76 , pp. 1101-1111
    • Müller, D.J.1    Fotiadis, D.2    Scheuring, S.3    Müller, S.A.4    Engel, A.5
  • 60
    • 0037099393 scopus 로고    scopus 로고
    • Conformational changes in surface structures of isolated connexin 26 gap junctions
    • Müller DJ, Hand GM, Engel A, Sosinsky G. 2002. Conformational changes in surface structures of isolated connexin 26 gap junctions. EMBO J. 21:3598-607
    • (2002) EMBO J , vol.21 , pp. 3598-3607
    • Müller, D.J.1    Hand, G.M.2    Engel, A.3    Sosinsky, G.4
  • 61
    • 0036932510 scopus 로고    scopus 로고
    • Stability of bacteriorhodopsin alpha-helices and loops analyzed by single-molecule force spectroscopy
    • Müller DJ, Kessler M, Oesterhelt F, Moeller C, Oesterhelt D, Gaub H. 2002. Stability of bacteriorhodopsin alpha-helices and loops analyzed by single-molecule force spectroscopy. Biophys. J. 83:3578-88
    • (2002) Biophys. J , vol.83 , pp. 3578-3588
    • Müller, D.J.1    Kessler, M.2    Oesterhelt, F.3    Moeller, C.4    Oesterhelt, D.5    Gaub, H.6
  • 63
    • 0036996692 scopus 로고    scopus 로고
    • Polar mutations in membrane proteins as a biophysical basis for disease
    • Partridge AW, Therien AG, Deber CM. 2002. Polar mutations in membrane proteins as a biophysical basis for disease. Biopolymers 66:350-58
    • (2002) Biopolymers , vol.66 , pp. 350-358
    • Partridge, A.W.1    Therien, A.G.2    Deber, C.M.3
  • 64
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot JL, Engelman DM. 1990. Membrane protein folding and oligomerization: the two-stage model. Biochemistry 29:4031-37
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 66
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief M, Gautel M, Oesterhelt F, Fernandez JM, Gaub HE. 1997. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276:1109-12
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 68
    • 29144532994 scopus 로고    scopus 로고
    • Characterizing molecular interactions in different bacteriorhodopsin assemblies by single-molecule force spectroscopy
    • Sapra KT, Besir H, Oesterhelt D, Muller DJ. 2006. Characterizing molecular interactions in different bacteriorhodopsin assemblies by single-molecule force spectroscopy. J. Mol. Biol. 355:640-50
    • (2006) J. Mol. Biol , vol.355 , pp. 640-650
    • Sapra, K.T.1    Besir, H.2    Oesterhelt, D.3    Muller, D.J.4
  • 73
    • 0036401862 scopus 로고    scopus 로고
    • The expanded denatured state: An ensemble of conformations trapped in a locally encoded topological space
    • Shortle D. 2002. The expanded denatured state: an ensemble of conformations trapped in a locally encoded topological space. Adv. Protein Chem. 62:1-23
    • (2002) Adv. Protein Chem , vol.62 , pp. 1-23
    • Shortle, D.1
  • 74
    • 0037031261 scopus 로고    scopus 로고
    • Effects of topology and excluded volume on protein denatured state conformational properties
    • Smith CR, Mateljevic N, Bowler BE. 2002. Effects of topology and excluded volume on protein denatured state conformational properties. Biochemistry 41:10173-81
    • (2002) Biochemistry , vol.41 , pp. 10173-10181
    • Smith, C.R.1    Mateljevic, N.2    Bowler, B.E.3
  • 76
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White SH, Wimley WC. 1999. Membrane protein folding and stability: physical principles. Annu. Rev. Biophys. Biomol. Struct. 28:319-65
    • (1999) Annu. Rev. Biophys. Biomol. Struct , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 77
    • 0030005250 scopus 로고    scopus 로고
    • Solvation energies of amino acid sidechains and backbone in a family of host-guest pentapeptides
    • Wimley WC, Creamer TP, White SH. 1996. Solvation energies of amino acid sidechains and backbone in a family of host-guest pentapeptides. Biochemistry 35:5109-24
    • (1996) Biochemistry , vol.35 , pp. 5109-5124
    • Wimley, W.C.1    Creamer, T.P.2    White, S.H.3
  • 78
    • 0034681908 scopus 로고    scopus 로고
    • Designing transmembrane alpha-helices that insert spontaneously
    • Wimley WC, White SH. 2000. Designing transmembrane alpha-helices that insert spontaneously. Biochemistry 39:4432-42
    • (2000) Biochemistry , vol.39 , pp. 4432-4442
    • Wimley, W.C.1    White, S.H.2
  • 80
    • 0007949690 scopus 로고    scopus 로고
    • Interhelical hydrogen bonding events drives strong interactions in membrane proteins
    • Zhou FX, Cocco MJ, Russ WP, Brunger AT, Engelman DM. 2000. Interhelical hydrogen bonding events drives strong interactions in membrane proteins. Nat. Struct. Biol. 7:154-60
    • (2000) Nat. Struct. Biol , vol.7 , pp. 154-160
    • Zhou, F.X.1    Cocco, M.J.2    Russ, W.P.3    Brunger, A.T.4    Engelman, D.M.5


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