메뉴 건너뛰기




Volumn 347, Issue 1, 2005, Pages 169-179

Sequence determinants of a transmembrane proton channel: An inverse relationship between stability and function

Author keywords

Analytical ultracentrifugation; Computer modeling; Influenza A virus; Proton channel; Thermodynamics

Indexed keywords

ALANINE; AMANTADINE; ION CHANNEL; MEMBRANE PROTEIN; OLIGOMER; PHENYLALANINE; PROTON; TETRAMER;

EID: 14144251553     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.01.023     Document Type: Article
Times cited : (56)

References (67)
  • 1
    • 4143085058 scopus 로고    scopus 로고
    • Folding of helical membrane proteins: The role of polar, GxxxG-like and proline motifs
    • A. Senes, D.E. Engel, and W.F. DeGrado Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs Curr. Opin. Struct. Biol. 14 2004 465 479
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 465-479
    • Senes, A.1    Engel, D.E.2    Degrado, W.F.3
  • 2
    • 0042931286 scopus 로고    scopus 로고
    • Sequence motifs, polar interactions and conformational changes in helical membrane proteins
    • A.R. Curran, and D.M. Engelman Sequence motifs, polar interactions and conformational changes in helical membrane proteins Curr. Opin. Struct. Biol. 13 2003 412 417
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 412-417
    • Curran, A.R.1    Engelman, D.M.2
  • 3
    • 0036226583 scopus 로고    scopus 로고
    • Comparison of helix interactions in membrane and soluble alpha-bundle proteins
    • M. Eilers, A.B. Patel, W. Liu, and S.O. Smith Comparison of helix interactions in membrane and soluble alpha-bundle proteins Biophys. J. 82 2002 2720 2736
    • (2002) Biophys. J. , vol.82 , pp. 2720-2736
    • Eilers, M.1    Patel, A.B.2    Liu, W.3    Smith, S.O.4
  • 5
    • 0032817780 scopus 로고    scopus 로고
    • Helix packing in polytopic membrane proteins: Role of glycine in transmembrane helix association
    • M.M. Javadpour, M. Eilers, M. Groesbeek, and S.O. Smith Helix packing in polytopic membrane proteins: role of glycine in transmembrane helix association Biophys. J. 77 1999 1609 1618
    • (1999) Biophys. J. , vol.77 , pp. 1609-1618
    • Javadpour, M.M.1    Eilers, M.2    Groesbeek, M.3    Smith, S.O.4
  • 6
    • 0035943429 scopus 로고    scopus 로고
    • Helix-helix packing and interfacial pairwise interactions of residues in membrane proteins
    • L. Adamian, and J. Liang Helix-helix packing and interfacial pairwise interactions of residues in membrane proteins J. Mol. Biol. 311 2001 891 907
    • (2001) J. Mol. Biol. , vol.311 , pp. 891-907
    • Adamian, L.1    Liang, J.2
  • 7
    • 0034711958 scopus 로고    scopus 로고
    • Statistical analysis of amino acid patterns in transmembrane helices: The GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions
    • A. Senes, M. Gerstein, and D.M. Engelman Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions J. Mol. Biol. 296 2000 921 936
    • (2000) J. Mol. Biol. , vol.296 , pp. 921-936
    • Senes, A.1    Gerstein, M.2    Engelman, D.M.3
  • 8
    • 0035979146 scopus 로고    scopus 로고
    • The Calpha-H...O hydrogen bond: A determinant of stability and specificity in transmembrane helix interactions
    • A. Senes, I. Ubarretxena-Belandia, and D.M. Engelman The Calpha-H...O hydrogen bond: a determinant of stability and specificity in transmembrane helix interactions Proc. Natl Acad. Sci. USA 98 2001 9056 9061
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 9056-9061
    • Senes, A.1    Ubarretxena-Belandia, I.2    Engelman, D.M.3
  • 9
    • 0037379072 scopus 로고    scopus 로고
    • How do helix-helix interactions help determine the folds of membrane proteins? Perspectives from the study of homo-oligomeric helical bundles
    • W.F. DeGrado, H. Gratkowski, and J.D. Lear How do helix-helix interactions help determine the folds of membrane proteins? Perspectives from the study of homo-oligomeric helical bundles Protein Sci. 12 2003 647 665
    • (2003) Protein Sci. , vol.12 , pp. 647-665
    • Degrado, W.F.1    Gratkowski, H.2    Lear, J.D.3
  • 10
    • 1642447793 scopus 로고    scopus 로고
    • Membrane proteins: A new method enters the fold
    • J.U. Bowie Membrane proteins: a new method enters the fold Proc. Natl Acad. Sci. USA 101 2004 3995 3996
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 3995-3996
    • Bowie, J.U.1
  • 11
    • 1642447757 scopus 로고    scopus 로고
    • Elastic coupling of integral membrane protein stability to lipid bilayer forces
    • H. Hong, and L.K. Tamm Elastic coupling of integral membrane protein stability to lipid bilayer forces Proc. Natl Acad. Sci. USA 101 2004 4065 4070
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 4065-4070
    • Hong, H.1    Tamm, L.K.2
  • 12
    • 0742288411 scopus 로고    scopus 로고
    • The evolution of transmembrane helix kinks and the structural diversity of G protein-coupled receptors
    • S. Yohannan, S. Faham, D. Yang, J.P. Whitelegge, and J.U. Bowie The evolution of transmembrane helix kinks and the structural diversity of G protein-coupled receptors Proc. Natl Acad. Sci. USA 101 2004 959 963
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 959-963
    • Yohannan, S.1    Faham, S.2    Yang, D.3    Whitelegge, J.P.4    Bowie, J.U.5
  • 15
    • 0001041988 scopus 로고    scopus 로고
    • Probing the folding and unfolding of wild-type and mutant forms of bacteriorhodopsin in micellar solutions: Evaluation of reversible unfolding conditions
    • G.Q. Chen, and E. Gouaux Probing the folding and unfolding of wild-type and mutant forms of bacteriorhodopsin in micellar solutions: evaluation of reversible unfolding conditions Biochemistry 38 1999 15380 15387
    • (1999) Biochemistry , vol.38 , pp. 15380-15387
    • Chen, G.Q.1    Gouaux, E.2
  • 16
    • 0033983453 scopus 로고    scopus 로고
    • Asparagine-mediated self-association of a model transmembrane helix
    • C. Choma, H. Gratkowski, J.D. Lear, and W.F. DeGrado Asparagine-mediated self-association of a model transmembrane helix Nature Struct. Biol. 7 2000 161 166
    • (2000) Nature Struct. Biol. , vol.7 , pp. 161-166
    • Choma, C.1    Gratkowski, H.2    Lear, J.D.3    Degrado, W.F.4
  • 17
    • 0035969998 scopus 로고    scopus 로고
    • Polar side-chains drive the association of model, transmembrane peptides
    • H. Gratkowski, J.D. Lear, and W.F. DeGrado Polar side-chains drive the association of model, transmembrane peptides Proc. Natl Acad. Sci. USA 98 2001 880 885
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 880-885
    • Gratkowski, H.1    Lear, J.D.2    Degrado, W.F.3
  • 20
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • J.-L. Popot, and D.M. Engelman Membrane protein folding and oligomerization: the two-stage model Biochemistry 29 1990 4031 4037
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.-L.1    Engelman, D.M.2
  • 21
    • 0033790343 scopus 로고    scopus 로고
    • Helical membrane protein folding, stability, and evolution
    • J.L. Popot, and D.M. Engelman Helical membrane protein folding, stability, and evolution Annu. Rev. Biochem. 69 2000 881 922
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 881-922
    • Popot, J.L.1    Engelman, D.M.2
  • 22
    • 0041914460 scopus 로고    scopus 로고
    • Determination of membrane protein stability via thermodynamic coupling of folding to thiol-disulfide interchange
    • L. Cristian, J.D. Lear, and W.F. DeGrado Determination of membrane protein stability via thermodynamic coupling of folding to thiol-disulfide interchange Protein Sci. 12 2003 1732 1740
    • (2003) Protein Sci. , vol.12 , pp. 1732-1740
    • Cristian, L.1    Lear, J.D.2    Degrado, W.F.3
  • 23
    • 0345598917 scopus 로고    scopus 로고
    • Use of thiol-disulfide equilibria to measure the energetics of assembly of transmembrane helices in phospholipid bilayers
    • L. Cristian, J.D. Lear, and W.F. DeGrado Use of thiol-disulfide equilibria to measure the energetics of assembly of transmembrane helices in phospholipid bilayers Proc. Natl Acad. Sci. USA 100 2003 14772 14777
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 14772-14777
    • Cristian, L.1    Lear, J.D.2    Degrado, W.F.3
  • 24
    • 0031956790 scopus 로고    scopus 로고
    • The dimerization motif of the glycophorin a transmembrane segment in membranes: Importance of glycine residues
    • B. Brosig, and D. Langosch The dimerization motif of the glycophorin A transmembrane segment in membranes: importance of glycine residues Protein Sci. 7 1998 1052 1056
    • (1998) Protein Sci. , vol.7 , pp. 1052-1056
    • Brosig, B.1    Langosch, D.2
  • 25
    • 0033514311 scopus 로고    scopus 로고
    • TOXCAT: A measure of transmembrane helix association in a biological membrane
    • W.P. Russ, and D.M. Engelman TOXCAT: a measure of transmembrane helix association in a biological membrane Proc. Natl Acad. Sci. USA 96 1999 863 868
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 863-868
    • Russ, W.P.1    Engelman, D.M.2
  • 26
    • 1342308081 scopus 로고    scopus 로고
    • Viral ion channels as models for ion transport and targets for antiviral drug action
    • L.H. Pinto, and R.A. Lamb Viral ion channels as models for ion transport and targets for antiviral drug action FEBS Letters 560 2004 1 2
    • (2004) FEBS Letters , vol.560 , pp. 1-2
    • Pinto, L.H.1    Lamb, R.A.2
  • 27
    • 0026785994 scopus 로고
    • The transmembrane domain of influenza a M2 protein forms amantadine-sensitive proton channels in planar lipid bilayers
    • K.C. Duff, and R.H. Ashley The transmembrane domain of influenza a M2 protein forms amantadine-sensitive proton channels in planar lipid bilayers Virology 190 1992 485 489
    • (1992) Virology , vol.190 , pp. 485-489
    • Duff, K.C.1    Ashley, R.H.2
  • 28
    • 0034700255 scopus 로고    scopus 로고
    • PH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza a virus
    • D. Salom, B.R. Hill, J.D. Lear, and W.F. DeGrado pH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus Biochemistry 39 2000 14160 14170
    • (2000) Biochemistry , vol.39 , pp. 14160-14170
    • Salom, D.1    Hill, B.R.2    Lear, J.D.3    Degrado, W.F.4
  • 29
    • 0034640212 scopus 로고    scopus 로고
    • Two possible conducting states of the influenza a virus M2 ion channel
    • Q. Zhong, D.M. Newns, P. Pattnaik, J.D. Lear, and M.L. Klein Two possible conducting states of the influenza A virus M2 ion channel FEBS Letters 473 2000 195 198
    • (2000) FEBS Letters , vol.473 , pp. 195-198
    • Zhong, Q.1    Newns, D.M.2    Pattnaik, P.3    Lear, J.D.4    Klein, M.L.5
  • 30
    • 3142716193 scopus 로고    scopus 로고
    • The computer simulation of proton transport in biomolecular systems
    • G.A. Voth The computer simulation of proton transport in biomolecular systems Front. Biosci. 8 2003 s1384 s1397
    • (2003) Front. Biosci. , vol.8
    • Voth, G.A.1
  • 31
    • 0034030929 scopus 로고    scopus 로고
    • Exploring models of the influenza a M2 channel: MD simulations in a phospholipid bilayer
    • L.R. Forrest, A. Kukol, I.T. Arkin, D.P. Tieleman, and M.S. Sansom Exploring models of the influenza A M2 channel: MD simulations in a phospholipid bilayer Biophys. J. 78 2000 55 69
    • (2000) Biophys. J. , vol.78 , pp. 55-69
    • Forrest, L.R.1    Kukol, A.2    Arkin, I.T.3    Tieleman, D.P.4    Sansom, M.S.5
  • 32
    • 0030881872 scopus 로고    scopus 로고
    • A functionally defined model for the M2 proton channel of influenza a virus suggests a mechanism for its ion selectivity
    • L.H. Pinto, G.R. Dieckmann, C.S. Gandhi, C.G. Papworth, J. Braman, and M.A. Shaughnessy A functionally defined model for the M2 proton channel of influenza A virus suggests a mechanism for its ion selectivity Proc. Natl Acad. Sci. USA 94 1997 11301 11306
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 11301-11306
    • Pinto, L.H.1    Dieckmann, G.R.2    Gandhi, C.S.3    Papworth, C.G.4    Braman, J.5    Shaughnessy, M.A.6
  • 34
    • 0033636640 scopus 로고    scopus 로고
    • Use of a single glycine residue to determine the tilt and orientation of a transmembrane helix. A new structural label for infrared spectroscopy [In Process Citation]
    • J. Torres, A. Kukol, and I.T. Arkin Use of a single glycine residue to determine the tilt and orientation of a transmembrane helix. A new structural label for infrared spectroscopy [In Process Citation] Biophys. J. 79 2000 3139 3143
    • (2000) Biophys. J. , vol.79 , pp. 3139-3143
    • Torres, J.1    Kukol, A.2    Arkin, I.T.3
  • 35
    • 0030777711 scopus 로고    scopus 로고
    • Transmembrane four-helix bundle of influenza a M2 protein channel: Structural implications from helix tilt and orientation
    • F.A. Kovacs, and T.A. Cross Transmembrane four-helix bundle of influenza A M2 protein channel: structural implications from helix tilt and orientation Biophys. J. 73 1997 2511 2517
    • (1997) Biophys. J. , vol.73 , pp. 2511-2517
    • Kovacs, F.A.1    Cross, T.A.2
  • 36
    • 0033073762 scopus 로고    scopus 로고
    • The influenza virus M2 ion channel protein: Probing the structure of the transmembrane domain in intact cells by using engineered disulfide cross-linking
    • C.M. Bauer, L.H. Pinto, T.A. Cross, and R.A. Lamb The influenza virus M2 ion channel protein: probing the structure of the transmembrane domain in intact cells by using engineered disulfide cross-linking Virology 254 1999 196 209
    • (1999) Virology , vol.254 , pp. 196-209
    • Bauer, C.M.1    Pinto, L.H.2    Cross, T.A.3    Lamb, R.A.4
  • 37
    • 0033868977 scopus 로고    scopus 로고
    • Transmembrane domain of M2 protein from influenza a virus studied by solid-state (15)N polarization inversion spin exchange at magic angle NMR
    • Z. Song, F.A. Kovacs, J. Wang, J.K. Denny, S.C. Shekar, J.R. Quine, and T.A. Cross Transmembrane domain of M2 protein from influenza A virus studied by solid-state (15)N polarization inversion spin exchange at magic angle NMR Biophys. J. 79 2000 767 775
    • (2000) Biophys. J. , vol.79 , pp. 767-775
    • Song, Z.1    Kovacs, F.A.2    Wang, J.3    Denny, J.K.4    Shekar, S.C.5    Quine, J.R.6    Cross, T.A.7
  • 38
    • 0034775070 scopus 로고    scopus 로고
    • Structure of the transmembrane region of the M2 protein H(+) channel
    • J. Wang, S. Kim, F. Kovacs, and T.A. Cross Structure of the transmembrane region of the M2 protein H(+) channel Protein Sci. 10 2001 2241 2250
    • (2001) Protein Sci. , vol.10 , pp. 2241-2250
    • Wang, J.1    Kim, S.2    Kovacs, F.3    Cross, T.A.4
  • 39
    • 0034614541 scopus 로고    scopus 로고
    • Helix tilt of the M2 transmembrane peptide from influenza a virus: An intrinsic property
    • F.A. Kovacs, J.K. Denny, Z. Song, J.R. Quine, and T.A. Cross Helix tilt of the M2 transmembrane peptide from influenza A virus: an intrinsic property J. Mol. Biol. 295 2000 117 125
    • (2000) J. Mol. Biol. , vol.295 , pp. 117-125
    • Kovacs, F.A.1    Denny, J.K.2    Song, Z.3    Quine, J.R.4    Cross, T.A.5
  • 40
    • 0037125949 scopus 로고    scopus 로고
    • Expression and initial structural insights from solid-state NMR of the M2 proton channel from influenza a virus
    • C. Tian, K. Tobler, R.A. Lamb, L.H. Pinto, and T.A. Cross Expression and initial structural insights from solid-state NMR of the M2 proton channel from influenza A virus Biochemistry 41 2002 11294 11300
    • (2002) Biochemistry , vol.41 , pp. 11294-11300
    • Tian, C.1    Tobler, K.2    Lamb, R.A.3    Pinto, L.H.4    Cross, T.A.5
  • 41
    • 0036787577 scopus 로고    scopus 로고
    • Uniformity, ideality, and hydrogen bonds in transmembrane alpha-helices
    • S. Kim, and T.A. Cross Uniformity, ideality, and hydrogen bonds in transmembrane alpha-helices Biophys. J. 83 2002 2084 2095
    • (2002) Biophys. J. , vol.83 , pp. 2084-2095
    • Kim, S.1    Cross, T.A.2
  • 42
    • 0142210121 scopus 로고    scopus 로고
    • Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers
    • C. Tian, P.F. Gao, L.H. Pinto, R.A. Lamb, and T.A. Cross Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers Protein Sci. 12 2003 2597 2605
    • (2003) Protein Sci. , vol.12 , pp. 2597-2605
    • Tian, C.1    Gao, P.F.2    Pinto, L.H.3    Lamb, R.A.4    Cross, T.A.5
  • 43
    • 0027103930 scopus 로고
    • Influence of amantadine resistance mutations on the pH regulatory function of the M2 protein of influenza a viruses
    • S. Grambas, M.S. Bennett, and A.J. Hay Influence of amantadine resistance mutations on the pH regulatory function of the M2 protein of influenza A viruses Virology 191 1992 541 549
    • (1992) Virology , vol.191 , pp. 541-549
    • Grambas, S.1    Bennett, M.S.2    Hay, A.J.3
  • 44
    • 0027185716 scopus 로고
    • Ion channel activity of influenza a virus M2 protein: Characterization of the amantadine block
    • C. Wang, K. Takeuchi, L.H. Pinto, and R.A. Lamb Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block J. Virol. 67 1993 5585 5594
    • (1993) J. Virol. , vol.67 , pp. 5585-5594
    • Wang, C.1    Takeuchi, K.2    Pinto, L.H.3    Lamb, R.A.4
  • 45
    • 0242721029 scopus 로고    scopus 로고
    • Assessment of development of resistance to antivirals in the ferret model of influenza virus infection
    • M.L. Herlocher, R. Truscon, R. Fenton, A. Klimov, S. Elias, S.E. Ohmit, and A.S. Monto Assessment of development of resistance to antivirals in the ferret model of influenza virus infection J. Infect. Dis. 188 2003 1355 1361
    • (2003) J. Infect. Dis. , vol.188 , pp. 1355-1361
    • Herlocher, M.L.1    Truscon, R.2    Fenton, R.3    Klimov, A.4    Elias, S.5    Ohmit, S.E.6    Monto, A.S.7
  • 46
    • 0037560121 scopus 로고    scopus 로고
    • High frequency of resistant viruses harboring different mutations in amantadine-treated children with influenza
    • K. Shiraishi, K. Mitamura, Y. Sakai-Tagawa, H. Goto, N. Sugaya, and Y. Kawaoka High frequency of resistant viruses harboring different mutations in amantadine-treated children with influenza J. Infect. Dis. 188 2003 57 61
    • (2003) J. Infect. Dis. , vol.188 , pp. 57-61
    • Shiraishi, K.1    Mitamura, K.2    Sakai-Tagawa, Y.3    Goto, H.4    Sugaya, N.5    Kawaoka, Y.6
  • 47
    • 0026004791 scopus 로고
    • Evolutionary analysis of the influenza a virus M gene with comparison of the M1 and M2 proteins
    • T. Ito, O.T. Gorman, Y. Kawaoka, W.J. Bean, and R.G. Webster Evolutionary analysis of the influenza A virus M gene with comparison of the M1 and M2 proteins J. Virol. 65 1991 5491 5498
    • (1991) J. Virol. , vol.65 , pp. 5491-5498
    • Ito, T.1    Gorman, O.T.2    Kawaoka, Y.3    Bean, W.J.4    Webster, R.G.5
  • 48
    • 0037172965 scopus 로고    scopus 로고
    • Sequence determinants of the energetics of folding of a transmembrane four-helix-bundle protein
    • K.P. Howard, J.D. Lear, and W.F. DeGrado Sequence determinants of the energetics of folding of a transmembrane four-helix-bundle protein Proc. Natl Acad. Sci. USA 99 2002 8568 8572
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 8568-8572
    • Howard, K.P.1    Lear, J.D.2    Degrado, W.F.3
  • 49
    • 0033554426 scopus 로고    scopus 로고
    • Total chemical synthesis of the integral membrane protein influenza a virus M2: Role of its C-terminal domain in tetramer assembly
    • G.G. Kochendoerfer, D. Salom, J.D. Lear, R. Wilk-Orescan, S.B. Kent, and W.F. DeGrado Total chemical synthesis of the integral membrane protein influenza A virus M2: role of its C-terminal domain in tetramer assembly Biochemistry 38 1999 11905 11913
    • (1999) Biochemistry , vol.38 , pp. 11905-11913
    • Kochendoerfer, G.G.1    Salom, D.2    Lear, J.D.3    Wilk-Orescan, R.4    Kent, S.B.5    Degrado, W.F.6
  • 50
    • 0034641749 scopus 로고    scopus 로고
    • Native protein sequences are close to optimal for their structures
    • B. Kuhlman, and D. Baker Native protein sequences are close to optimal for their structures Proc. Natl Acad. Sci. USA 97 2000 10383 10388
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 10383-10388
    • Kuhlman, B.1    Baker, D.2
  • 52
    • 0034493023 scopus 로고    scopus 로고
    • Evolution of binding affinity in a WW domain probed by phage display
    • P.A. Dalby, R.H. Hoess, and W.F. DeGrado Evolution of binding affinity in a WW domain probed by phage display Protein Sci. 9 2000 2366 2376
    • (2000) Protein Sci. , vol.9 , pp. 2366-2376
    • Dalby, P.A.1    Hoess, R.H.2    Degrado, W.F.3
  • 53
    • 0035807810 scopus 로고    scopus 로고
    • Specificity in transmembrane helix-helix interactions can define a hierarchy of stability for sequence variants
    • K.G. Fleming, and D.M. Engelman Specificity in transmembrane helix-helix interactions can define a hierarchy of stability for sequence variants Proc. Natl Acad. Sci. USA 98 2001 14340 14344
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 14340-14344
    • Fleming, K.G.1    Engelman, D.M.2
  • 54
  • 56
    • 0035423934 scopus 로고    scopus 로고
    • Stabilizing membrane proteins
    • J.U. Bowie Stabilizing membrane proteins Curr. Opin. Struct. Biol. 11 2001 397 402
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 397-402
    • Bowie, J.U.1
  • 57
    • 0030777759 scopus 로고    scopus 로고
    • The effect of point mutations on the free energy of transmembrane alpha-helix dimerization
    • K.G. Fleming, A.L. Ackerman, and D.M. Engelman The effect of point mutations on the free energy of transmembrane alpha-helix dimerization J. Mol. Biol. 272 1997 266 275
    • (1997) J. Mol. Biol. , vol.272 , pp. 266-275
    • Fleming, K.G.1    Ackerman, A.L.2    Engelman, D.M.3
  • 60
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: A framework for transmembrane helix-helix association
    • W.P. Russ, and D.M. Engelman The GxxxG motif: a framework for transmembrane helix-helix association J. Mol. Biol. 296 2000 911 919
    • (2000) J. Mol. Biol. , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 61
    • 0016218601 scopus 로고
    • Molecular characterization of proteins in detergent solutions
    • C. Tanford, Y. Nozaki, J.A. Reynolds, and S. Makino Molecular characterization of proteins in detergent solutions Biochemistry 13 1974 2369 2376
    • (1974) Biochemistry , vol.13 , pp. 2369-2376
    • Tanford, C.1    Nozaki, Y.2    Reynolds, J.A.3    Makino, S.4
  • 62
    • 0345304457 scopus 로고    scopus 로고
    • Computational design and characterization of a monomeric helical dinuclear metalloprotein
    • J.R. Calhoun, H. Kono, S. Lahr, W. Wang, W.F. DeGrado, and J.G. Saven Computational design and characterization of a monomeric helical dinuclear metalloprotein J. Mol. Biol. 334 2003 1101 1115
    • (2003) J. Mol. Biol. , vol.334 , pp. 1101-1115
    • Calhoun, J.R.1    Kono, H.2    Lahr, S.3    Wang, W.4    Degrado, W.F.5    Saven, J.G.6
  • 63
    • 0035577805 scopus 로고    scopus 로고
    • A new data analysis method to determine binding constants of small molecules to proteins using equilibrium analytical ultracentrifugation with absorption optics
    • M. Arkin, and J.D. Lear A new data analysis method to determine binding constants of small molecules to proteins using equilibrium analytical ultracentrifugation with absorption optics Anal. Biochem. 299 2001 98 107
    • (2001) Anal. Biochem. , vol.299 , pp. 98-107
    • Arkin, M.1    Lear, J.D.2
  • 64
    • 0031576989 scopus 로고    scopus 로고
    • Prediction of protein side-chain rotamers from a backbone-dependent rotamer library: A new homology modeling tool
    • M.J. Bower, F.E. Cohen, and R.L. Dunbrack Prediction of protein side-chain rotamers from a backbone-dependent rotamer library: A new homology modeling tool J. Mol. Biol. 267 1997 1268 1282
    • (1997) J. Mol. Biol. , vol.267 , pp. 1268-1282
    • Bower, M.J.1    Cohen, F.E.2    Dunbrack, R.L.3
  • 65
    • 0026589733 scopus 로고
    • The dead-end elimination theorem and its use in protein side-chain positioning
    • J. Desmet, M. De Maeyer, B. Hazes, and I. Lasters The dead-end elimination theorem and its use in protein side-chain positioning Nature 356 1992 539 542
    • (1992) Nature , vol.356 , pp. 539-542
    • Desmet, J.1    De Maeyer, M.2    Hazes, B.3    Lasters, I.4
  • 66
    • 0028212927 scopus 로고
    • Efficient rotamer elimination applied to protein side-chains and related spin glasses
    • R.F. Goldstein Efficient rotamer elimination applied to protein side-chains and related spin glasses Biophys. J. 66 1994 1335 1340
    • (1994) Biophys. J. , vol.66 , pp. 1335-1340
    • Goldstein, R.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.