메뉴 건너뛰기




Volumn 247, Issue 4, 1995, Pages 808-822

The effect of environment on the stability of an integral membrane helix: Molecular dynamics simulations of surfactant protein C in chloroform, methanol and water

Author keywords

Computer simulation; Molecular dynamics; Peptide conformation; Solvent interactions; helix stability

Indexed keywords

CHLOROFORM; LUNG SURFACTANT; METHANOL; PROTEIN C; VALINE; WATER;

EID: 0028904088     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(05)80156-1     Document Type: Article
Times cited : (73)

References (59)
  • 1
    • 0027090063 scopus 로고
    • Structure and functions of a dimeric form of surfactant protein SP-C: A Fourier transform infrared and surfactometry study
    • Baatz, J. E., Smyth, K. L. Whitsett, J. A., Baxter, C. & Absolom, D. R. (1992). Structure and functions of a dimeric form of surfactant protein SP-C: a Fourier transform infrared and surfactometry study. Chem. Phys. Lipids, 63, 91-104.
    • (1992) Chem. Phys. Lipids , vol.63 , pp. 91-104
    • Baatz, J.E.1    Smyth, K.L.2    Whitsett, J.A.3    Baxter, C.4    Absolom, D.R.5
  • 2
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration
    • Pullman, B., ed.), Reidel, Dordrecht
    • Berendsen, H. J. C., Postma, J. P. M., van Gunsteren, W. F. & Hermans, J. (1981). Interaction models for water in relation to protein hydration. In Intermolecular Forces (Pullman, B., ed.), pp. 331-342, Reidel, Dordrecht.
    • (1981) Intermolecular Forces , pp. 331-342
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Van Gunsteren, W.F.3    Hermans, J.4
  • 4
    • 0027236794 scopus 로고
    • Structural basis of amino acid a-helix propensity
    • Blaber, M., Zhang, X.-J. & Matthews, B. W. (1993). Structural basis of amino acid a-helix propensity. Science, 260, 1637-1640.
    • (1993) Science , vol.260 , pp. 1637-1640
    • Blaber, M.1    Zhang, X.-J.2    Matthews, B.W.3
  • 6
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou, P. Y. & Fasman, G. D. (1978). Prediction of the secondary structure of proteins from their amino acid sequence. Advan. Enzymol. 47, 45-148.
    • (1978) Advan. Enzymol. , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 7
    • 0026665778 scopus 로고
    • Side-chain entropy opposes a-helix formation but rationalizes experimentally determined helix-forming propensities
    • Creamer, R. P. & Rose, G. D. (1992). Side-chain entropy opposes a-helix formation but rationalizes experimentally determined helix-forming propensities. Proc. Nat. Acad. Sci., U.S.A. 89, 5937-5941.
    • (1992) Proc. Nat. Acad. Sci., U.S.A. , vol.89 , pp. 5937-5941
    • Creamer, R.P.1    Rose, G.D.2
  • 9
    • 0025239383 scopus 로고
    • Hydrophobic surfactant-associated polypeptides: SPC is a lipopeptide with two palmitoylated cysteine residues, whereas SP-B lacks covalently linked fatty acyl groups
    • Curstedt, T., Johansson, J., Persson, P., Eklund, A., Robertson, B., Lowenadler, B. & Jornvall, H. (1990). Hydrophobic surfactant-associated polypeptides: SPC is a lipopeptide with two palmitoylated cysteine residues, whereas SP-B lacks covalently linked fatty acyl groups. Proc. Nat. Acad. Sci., U.S.A. 87, 2985-2989.
    • (1990) Proc. Nat. Acad. Sci., U.S.A. , vol.87 , pp. 2985-2989
    • Curstedt, T.1    Johansson, J.2    Persson, P.3    Eklund, A.4    Robertson, B.5    Lowenadler, B.6    Jornvall, H.7
  • 10
    • 0026525048 scopus 로고
    • Molecular dynamics simulations of helix denaturation
    • Daggett, V. & Levitt, M. (1992). Molecular dynamics simulations of helix denaturation. J. Mol. Biol. 223, 1121-1138.
    • (1992) J. Mol. Biol. , vol.223 , pp. 1121-1138
    • Daggett, V.1    Levitt, M.2
  • 11
    • 0000341366 scopus 로고
    • Molecular dynamics simulation of galanin in aqueous and non-aqueous solution
    • De Loof, H., Nilsson, L. & Rigler, R. (1992). Molecular dynamics simulation of galanin in aqueous and non-aqueous solution.J. Amer. Chem. Soc. 114, 4028-4035.
    • (1992) J. Amer. Chem. Soc , vol.114 , pp. 4028-4035
    • De Loof, H.1    Nilsson, L.2    Rigler, R.3
  • 12
    • 0000269886 scopus 로고
    • Theoretical evidence for water insertion in a-helix bending: Molecular dynamics of Gly30 and Ala30 in vacuo and in solution
    • DiCapua, F. M., Swaminathan, S. & Beveridge, D. L. (1991). Theoretical evidence for water insertion in a-helix bending: molecular dynamics of Gly30 and Ala30 in vacuo and in solution. J. Amer. Chem. Soc. 113, 6145-6155.
    • (1991) J. Amer. Chem. Soc. , vol.113 , pp. 6145-6155
    • Dicapua, F.M.1    Swaminathan, S.2    Beveridge, D.L.3
  • 13
    • 0021446362 scopus 로고
    • Structure of liquid chloroform. A comparison between computer simulation and neutron scattering results
    • Dietz, W. & Heinzinger, K. (1984). Structure of liquid chloroform. A comparison between computer simulation and neutron scattering results. Ber. Bunsenges. Phys. Chem. 88, 543-546.
    • (1984) Ber. Bunsenges. Phys. Chem. , vol.88 , pp. 543-546
    • Dietz, W.1    Heinzinger, K.2
  • 14
    • 0001740476 scopus 로고
    • A molecular dynamics study of liquid chloroform
    • Dietz, W. & Heinzinger, K. (1985). A molecular dynamics study of liquid chloroform. Berg. Bunsenges. Phys. Chem. 89, 968-977.
    • (1985) Berg. Bunsenges. Phys. Chem. , vol.89 , pp. 968-977
    • Dietz, W.1    Heinzinger, K.2
  • 15
    • 0027141121 scopus 로고
    • Solvent-dependent conformation and hydrogen-bonding capacity of cyclosporin A: Evidence from partition coefficients and molecular dynamics simulations
    • El Tayar, N., Mark, A. E., Vallat, P., Brunne, R. M., Testa, B. & van Gunsteren, W. F. (1993). Solvent-dependent conformation and hydrogen-bonding capacity of cyclosporin A: evidence from partition coefficients and molecular dynamics simulations. J. Med. Chem. 36, 3757-3764.
    • (1993) J. Med. Chem. , vol.36 , pp. 3757-3764
    • El Tayar, N.1    Mark, A.E.2    Vallat, P.3    Brunne, R.M.4    Testa, B.5    Van Gunsteren, W.F.6
  • 17
    • 0026058806 scopus 로고
    • Physical reasons for secondary structure stability: A-helices in short peptides
    • Finkeistein, A. V., Badretdinov, A. Y. & Ptitsyn, O. B. (1991). Physical reasons for secondary structure stability: a-helices in short peptides. Proteins: Struct. Fund. Genet. 10, 287-299.
    • (1991) Proteins: Struct. Fund. Genet. , vol.10 , pp. 287-299
    • Finkeistein, A.V.1    Badretdinov, A.Y.2    Ptitsyn, O.B.3
  • 18
    • 0001159492 scopus 로고
    • Protein dynamics and solvation in aqueous and nonaqueous environments
    • Hartsough, D. S. & Merz, K. M., Jr (1993). Protein dynamics and solvation in aqueous and nonaqueous environments. J. Amer. Chem. Soc. 115, 6529-6537.
    • (1993) J. Amer. Chem. Soc. , vol.115 , pp. 6529-6537
    • Hartsough, D.S.1    Merz, K.M.2
  • 19
    • 0003742069 scopus 로고
    • Department of Biochemistry and Molecular Biology, University College, London, U.K
    • Hubbard, S. J. & Thornton, J. M. (1993). "Naccess", Computer Program, Department of Biochemistry and Molecular Biology, University College, London, U.K.
    • (1993) Naccess Computer Program
    • Hubbard, S.J.1    Thornton, J.M.2
  • 20
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. & Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers, 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 21
    • 0023893969 scopus 로고
    • Size and structure of the hydrophobic low molecular weight surfactant-associated polypeptide
    • Johansson, J., Curstedt, T., Robertson, B. & Jörnvall, H. (1988). Size and structure of the hydrophobic low molecular weight surfactant-associated polypeptide. Biochemistry, 27, 3544-3547.
    • (1988) Biochemistry , vol.27 , pp. 3544-3547
    • Johansson, J.1    Curstedt, T.2    Robertson, B.3    Jörnvall, H.4
  • 23
    • 0028358907 scopus 로고
    • The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich a-helix
    • Johansson, J., Szyperski, T., Curstedt, T. & Wüthrich, K. (1994a). The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich a-helix. Biochemistry, 33, 6015-6023.
    • (1994) Biochemistry , vol.33 , pp. 6015-6023
    • Johansson, J.1    Szyperski, T.2    Curstedt, T.3    Wüthrich, K.4
  • 24
    • 85027592628 scopus 로고
    • A structural basis for the function of the pulmonary surfactant-associated polypeptide SP-C
    • the press
    • Johansson, J., Szyperski, T. & Wüthrich, K. (1995a). A structural basis for the function of the pulmonary surfactant-associated polypeptide SP-C. FEBS Letters, in the press.
    • (1995) FEBS Letters
    • Johansson, J.1    Szyperski, T.2    Wüthrich, K.3
  • 25
    • 0028958502 scopus 로고
    • Secondary structure and biophysical activity of synthetic analogs of the pulmonary surfactant polypeptide SPC
    • the press
    • Johansson, J., Nilsson, G., Strömberg, R., Robertson, B., Jörnvall, H. & Curstedt, T. (1995). Secondary structure and biophysical activity of synthetic analogs of the pulmonary surfactant polypeptide SPC. Biochem. J. In the press.
    • (1995) Biochem. J
    • Johansson, J.1    Nilsson, G.2    Strömberg, R.3    Robertson, B.4    Jörnvall, H.5    Curstedt, T.6
  • 26
    • 0025375637 scopus 로고
    • On the dependence of molecular conformation on the type of solvent environment: A molecular dynamics study of cyclosporin A
    • Lautz, J., Kessler, H., van Gunsteren, W. F., Weber, H.-P. & Wenger, R. M. (1990). On the dependence of molecular conformation on the type of solvent environment: a molecular dynamics study of cyclosporin A. Biopolymers, 29, 1669-1687.
    • (1990) Biopolymers , vol.29 , pp. 1669-1687
    • Lautz, J.1    Kessler, H.2    Van Gunsteren, W.F.3    Weber, H.-P.4    Wenger, R.M.5
  • 28
    • 0025260032 scopus 로고
    • Side-chain contributions to the stability of alpha-helical structure in peptides
    • Lyu, P. C., Liff, M. I., Marky, L. A. & Kallenbach, N. R. (1990). Side-chain contributions to the stability of alpha-helical structure in peptides. Science, 250, 669-673.
    • (1990) Science , vol.250 , pp. 669-673
    • Lyu, P.C.1    Liff, M.I.2    Marky, L.A.3    Kallenbach, N.R.4
  • 29
    • 0026018050 scopus 로고
    • A-Helix stabilization by natural and unnatural amino acids with alkyl side chains
    • Lyu, P. C., Sherman, J. C., Chen, A. & Kallenbach, N. R. (1991). a-Helix stabilization by natural and unnatural amino acids with alkyl side chains. Proc. Nat. Acad. Sei., U.S.A. 88, 5317-5320.
    • (1991) Proc. Nat. Acad. Sei., U.S.A. , vol.88 , pp. 5317-5320
    • Lyu, P.C.1    Sherman, J.C.2    Chen, A.3    Kallenbach, N.R.4
  • 30
    • 0026630480 scopus 로고
    • Simulation of the thermal denaturation of hen egg white lysozyme: Trapping the molten globule state
    • Mark, A. E. & van Gunsteren, W. F. (1992). Simulation of the thermal denaturation of hen egg white lysozyme: trapping the molten globule state. Biochemistry, 31, 7745-7748.
    • (1992) Biochemistry , vol.31 , pp. 7745-7748
    • Mark, A.E.1    Van Gunsteren, W.F.2
  • 31
    • 0008025298 scopus 로고
    • Convergence properties of free energy calculations: A-cyclodextrin complexes as a case study
    • Mark, A. E., van Helden, S. P., Smith, P. E., Janssen, L. H. M. & van Gunsteren, W. F. (1994). Convergence properties of free energy calculations: a-cyclodextrin complexes as a case study J. Amer. Chem. Soc. 116, 6293-6302.
    • (1994) J. Amer. Chem. Soc , vol.116 , pp. 6293-6302
    • Mark, A.E.1    Van Helden, S.P.2    Smith, P.E.3    Janssen, L.H.M.4    Van Gunsteren, W.F.5
  • 32
    • 0023521842 scopus 로고
    • Analysis of the relationship between side-chain conformation and secondary structure in globular proteins
    • McGregor, M. J., Islam, S. A. & Sternberg, M. J. E. (1987). Analysis of the relationship between side-chain conformation and secondary structure in globular proteins. /. Mo!. Biol. 198, 295-310.
    • (1987) Mol. Biol. , vol.198 , pp. 295-310
    • McGregor, M.J.1    Islam, S.A.2    Sternberg, M.J.E.3
  • 33
    • 0024997237 scopus 로고
    • Effect of central-residue replacements on the helical stability of a monomeric peptide
    • Merutka, G., Lipton, W., Shalongo, W., Park, S.-H. & Stellwagen, E. (1990). Effect of central-residue replacements on the helical stability of a monomeric peptide. Biochemistry, 29, 7511-7515.
    • (1990) Biochemistry , vol.29 , pp. 7511-7515
    • Merutka, G.1    Lipton, W.2    Shalongo, W.3    Park, S.-H.4    Stellwagen, E.5
  • 34
    • 0001425970 scopus 로고
    • Molecular dynamics with dimethyl sulfoxide as a solvent. Conformation of a cyclic hexapeptide
    • Mierke, D. F. & Kessler, H. (1991). Molecular dynamics with dimethyl sulfoxide as a solvent. Conformation of a cyclic hexapeptide.J. Amer. Chem. Soc. 113, 9466-9470.
    • (1991) J. Amer. Chem. Soc , vol.113 , pp. 9466-9470
    • Mierke, D.F.1    Kessler, H.2
  • 35
    • 0028146056 scopus 로고
    • Molecular dynamics simulations of an enzyme surrounded by vacuum, water, or a hydrophobic solvent
    • Norin, M., Haeffner, F., Hult, K. & Edholm, O. (1994). Molecular dynamics simulations of an enzyme surrounded by vacuum, water, or a hydrophobic solvent. Bioplnls. J. 67, 548-559.
    • (1994) Bioplnls. J. , vol.67 , pp. 548-559
    • Norin, M.1    Haeffner, F.2    Hult, K.3    Edholm, O.4
  • 36
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occuring amino acids
    • O'Neil, K. T. & DeGrado, W. F. (1990). A thermodynamic scale for the helix-forming tendencies of the commonly occuring amino acids. Science, 250, 646-651.
    • (1990) Science , vol.250 , pp. 646-651
    • O'neil, K.T.1    Degrado, W.F.2
  • 38
    • 0028142385 scopus 로고
    • Helix-forming tendencies of amino acids in short (Hydroxybutyl-L-glutamine peptides: An evaluation of the contradictory results from host-guest studies and short alanine-based peptides
    • Padmanabhan, S., York, E. J., Gera, L., Stewart, J. M. & Baldwin, R. L. (1994). Helix-forming tendencies of amino acids in short (hydroxybutyl-L-glutamine peptides: an evaluation of the contradictory results from host-guest studies and short alanine-based peptides. Biochemistry, 33, 8604-8609.
    • (1994) Biochemistry , vol.33 , pp. 8604-8609
    • Padmanabhan, S.1    York, E.J.2    Gera, L.3    Stewart, J.M.4    Baldwin, R.L.5
  • 39
    • 0021764813 scopus 로고
    • Calibration of the angular dependence of the amide proton-C" proton coupling constants, 7hn„ in a globular protein
    • Pardi, A., Billeter, M. & Wuthrich, K. (1984). Calibration of the angular dependence of the amide proton-C" proton coupling constants, 7hn„ in a globular protein. J. Mol. Biol. 180, 741-751.
    • (1984) J. Mol. Biol. , vol.180 , pp. 741-751
    • Pardi, A.1    Billeter, M.2    Wuthrich, K.3
  • 40
    • 0025999791 scopus 로고
    • Fourier transform infrared studies of secondary structure and orientation of pulmonary surfactant protein SP-C and its effect on the dynamic surface properties of phospholipids
    • Pastrana, B., Mautone, A. J. & Mendelsohn, R. (1991). Fourier transform infrared studies of secondary structure and orientation of pulmonary surfactant protein SP-C and its effect on the dynamic surface properties of phospholipids. Biochemistry, 30, 10058-10064.
    • (1991) Biochemistry , vol.30 , pp. 10058-10064
    • Pastrana, B.1    Mautone, A.J.2    Mendelsohn, R.3
  • 41
    • 0027264459 scopus 로고
    • Integral membrane protein structure: Transmembrane a-heiices as autonomous folding domains
    • Popot, J.-L. (1993). Integral membrane protein structure: transmembrane a-heiices as autonomous folding domains. Curr. Opin. Struct. Biol. 3, 532-540.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 532-540
    • Popot, J.-L.1
  • 43
    • 33646940952 scopus 로고
    • Numerical integration of cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, j.-P., Ciccotti, G. & Berendsen, H. J. C. (1977). Numerical integration of cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. /. Comp. Phys. 23, 327-341.
    • (1977) Comp. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 44
    • 0026755515 scopus 로고
    • Cutoff size does strongly influence molecular dynamics results on solvated polypeptides
    • Schreiber, H. & Steinhauser, O. (1992). Cutoff size does strongly influence molecular dynamics results on solvated polypeptides. Biochemistry, 31, 5856-5860.
    • (1992) Biochemistry , vol.31 , pp. 5856-5860
    • Schreiber, H.1    Steinhauser, O.2
  • 45
    • 84948512335 scopus 로고
    • On the approximation of solvent effects on the conformation and dynamics of cyclosporin A by stochastic dynamics simulation techniques
    • Shi, Y.-Y., Wang, L. & van Gunsteren, W. F. (1988). On the approximation of solvent effects on the conformation and dynamics of cyclosporin A by stochastic dynamics simulation techniques. Mol. Simulai. 1, 369-383.
    • (1988) Mol. Simulai. , vol.1 , pp. 369-383
    • Shi, Y.-Y.1    Wang, L.2    Van Gunsteren, W.F.3
  • 46
    • 0027135626 scopus 로고
    • Free energy profile of a 3m- to a-helical transition of an oligopeptide in various solvents
    • Smythe, M. L., Huston, S. E. & Marshall, G. R. (1993). Free energy profile of a 3m- to a-helical transition of an oligopeptide in various solvents. J. Amer. Chem. Soc. 115, 11594-11595.
    • (1993) J. Amer. Chem. Soc , vol.115 , pp. 11594-11595
    • Smythe, M.L.1    Huston, S.E.2    Marshall, G.R.3
  • 47
    • 0026237127 scopus 로고
    • Unfolding of an a-helix in water
    • Soman, K. V., Karimi, A. & Case, D. A. (1991). Unfolding of an a-helix in water. Biopolymers, 31, 1351-1361.
    • (1991) Biopolymers , vol.31 , pp. 1351-1361
    • Soman, K.V.1    Karimi, A.2    Case, D.A.3
  • 49
    • 0025858688 scopus 로고
    • Molecular dynamics simulations of the unfolding of an a-helical analogue of ribonuclease A S-peptide in water
    • Tirado-Rives, J. & Jorgensen, W. L. (1991). Molecular dynamics simulations of the unfolding of an a-helical analogue of ribonuclease A S-peptide in water. Biochemistry, 30, 3864-3871.
    • (1991) Biochemistry , vol.30 , pp. 3864-3871
    • Tirado-Rives, J.1    Jorgensen, W.L.2
  • 50
    • 0025767212 scopus 로고
    • Thermodynamics and mechanism of a-helix initiation in alanine and valine peptides
    • Tobias, D. J. & Brooks, C. L., III (1991). Thermodynamics and mechanism of a-helix initiation in alanine and valine peptides. Biochemistry, 30, 6059-6070.
    • (1991) Biochemistry , vol.30 , pp. 6059-6070
    • Tobias, D.J.1    Brooks, C.L.2
  • 51
    • 36749110658 scopus 로고
    • Dipolar relaxation and nuclear Overhauser effects in nonrigid molecules: The effect of fluctuating internuclear distances
    • Tropp, J. (1980). Dipolar relaxation and nuclear Overhauser effects in nonrigid molecules: the effect of fluctuating internuclear distances. J. Chem. Plns. 72, 6035-6043.
    • (1980) J. Chem. Plns , vol.72 , pp. 6035-6043
    • Tropp, J.1
  • 52
    • 0027642798 scopus 로고
    • Molecular dynamics simulation of the stability of a 22-residue a-helix in water and 30% trifluoroethanol
    • van Buuren, A. R. & Berendsen, H. J. C. (1993). Molecular dynamics simulation of the stability of a 22-residue a-helix in water and 30% trifluoroethanol. Biopolymers, 33, 1159-1166.
    • (1993) Biopolymers , vol.33 , pp. 1159-1166
    • Van Buuren, A.R.1    Berendsen, H.J.C.2
  • 55
    • 2142813682 scopus 로고
    • Computer simulation of molecular dynamics: Methodology, applications and perspectives in chemistry
    • van Gunsteren, W. F. & Berendsen, H. J. C. (1990). Computer simulation of molecular dynamics: methodology, applications and perspectives in chemistry. Angeio. Chem. Int. Ed. Engl. 29, 992-1023.
    • (1990) Angeio. Chem. Int. Ed. Engl. , vol.29 , pp. 992-1023
    • Van Gunsteren, W.F.1    Berendsen, H.J.C.2
  • 56
    • 0020480264 scopus 로고
    • Protein dynamics in solution and in a crystalline environment: A molecular dynamics study
    • van Gunsteren, W. F. & Karplus, M. (1982). Protein dynamics in solution and in a crystalline environment: a molecular dynamics study. Biochemistry, 21, 2259-2274.
    • (1982) Biochemistry , vol.21 , pp. 2259-2274
    • Van Gunsteren, W.F.1    Karplus, M.2
  • 57
    • 0025113815 scopus 로고
    • Helix-coil stability constants for the naturally occuring amino acids in water. XXIV. Half-cystine parameters from random poly(hydroxybutylglu-tamine-co-S-methylthio-L-cystein)
    • Wójcik, J., Altmann, K.-H. & Scheraga, H. A. (1990). Helix-coil stability constants for the naturally occuring amino acids in water. XXIV. Half-cystine parameters from random poly(hydroxybutylglu-tamine-co-S-methylthio-L-cystein). Biopolymers, 30, 121-134.
    • (1990) Biopolymers , vol.30 , pp. 121-134
    • Wójcik, J.1    Altmann, K.-H.2    Scheraga, H.A.3
  • 58
    • 0026050172 scopus 로고
    • Conformational equilibria of valine studies by dynamics simulation
    • Yun, R. H. & Hermans, J. (1991). Conformational equilibria of valine studies by dynamics simulation. Protein Eng. 4, 761-766.
    • (1991) Protein Eng , vol.4 , pp. 761-766
    • Yun, R.H.1    Hermans, J.2
  • 59
    • 0000668407 scopus 로고
    • Theory of the phase transition between helix and random coil in polypeptide chains
    • Zimm, B. H. & Bragg, J. K. (1959). Theory of the phase transition between helix and random coil in polypeptide chains. J. Chem. Phys. 31, 526-535.
    • (1959) J. Chem. Phys. , vol.31 , pp. 526-535
    • Zimm, B.H.1    Bragg, J.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.