메뉴 건너뛰기




Volumn 25, Issue 2, 1996, Pages 202-214

Molecular dynamics simulations of synthetic peptide folding

Author keywords

helical ratio; hydrophobic interaction; multiple minima problem; side chain backbone hydrogen bonding; single residue substitution; solvent referenced potential

Indexed keywords

HELIX LOOP HELIX PROTEIN;

EID: 0030006074     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199606)25:2<202::AID-PROT6>3.0.CO;2-J     Document Type: Article
Times cited : (56)

References (73)
  • 1
    • 0016696599 scopus 로고
    • Studies on protein folding, unfolding and fluctuations by computer simulation
    • Taketomi, H., Ueda, Y., Go, N. Studies on protein folding, unfolding and fluctuations by computer simulation. Int. J. Peptide Protein Res. 7:445-459, 1975.
    • (1975) Int. J. Peptide Protein Res. , vol.7 , pp. 445-459
    • Taketomi, H.1    Ueda, Y.2    Go, N.3
  • 2
    • 0022423920 scopus 로고
    • Theory for the folding and stability of globular proteins
    • Dill, K. Theory for the folding and stability of globular proteins. Biochemistry 24:1501-1509, 1985.
    • (1985) Biochemistry , vol.24 , pp. 1501-1509
    • Dill, K.1
  • 3
    • 0025608908 scopus 로고
    • Simulations of the folding of a globular protein
    • Skolnick, J., Kolinski, A. Simulations of the folding of a globular protein. Science 250:1121-1125, 1990.
    • (1990) Science , vol.250 , pp. 1121-1125
    • Skolnick, J.1    Kolinski, A.2
  • 4
    • 0025809473 scopus 로고
    • Influence of point mutations on protein structure: Probability of a neutral mutation
    • Shakhnovich, E.I., Gutin, A.M. Influence of point mutations on protein structure: Probability of a neutral mutation. J. Theor. Biol. 149:537-546, 1991.
    • (1991) J. Theor. Biol. , vol.149 , pp. 537-546
    • Shakhnovich, E.I.1    Gutin, A.M.2
  • 5
    • 0026107642 scopus 로고
    • Molecular dynamics simulations of small peptides: Dependence on dielectric model and pH
    • Daggett, V., Kolhnan, P.A., Kuntz, I.D. Molecular dynamics simulations of small peptides: Dependence on dielectric model and pH. Biopolymers 31:285-304, 1991.
    • (1991) Biopolymers , vol.31 , pp. 285-304
    • Daggett, V.1    Kolhnan, P.A.2    Kuntz, I.D.3
  • 7
    • 0024066560 scopus 로고
    • On the multiple-minima problem in the conformational analysis of polypeptides. II. An electrostatically driven Monte Carlo method - Tests on poly(l-alanine)
    • Ripoll, D.R., Scheraga, H.A. On the multiple-minima problem in the conformational analysis of polypeptides. II. An electrostatically driven Monte Carlo method - tests on poly(l-alanine). Biopolymers 27:1283-1303, 1988.
    • (1988) Biopolymers , vol.27 , pp. 1283-1303
    • Ripoll, D.R.1    Scheraga, H.A.2
  • 8
    • 0025164892 scopus 로고
    • Applications of simulated annealing to peptides
    • Wilson, S.R., Cui, W. Applications of simulated annealing to peptides. Biopolymers 29:225-235, 1990.
    • (1990) Biopolymers , vol.29 , pp. 225-235
    • Wilson, S.R.1    Cui, W.2
  • 9
    • 0025850527 scopus 로고
    • α-helix folding by Monte Carlo simulated annealing in isolated C-peptide of ribonmuclease A
    • Okamoto Y., Fukugita M., Nakazawa T., Kawai H. α-helix folding by Monte Carlo simulated annealing in isolated C-peptide of ribonmuclease A. Protein Eng. 4:639-647, 1991.
    • (1991) Protein Eng. , vol.4 , pp. 639-647
    • Okamoto, Y.1    Fukugita, M.2    Nakazawa, T.3    Kawai, H.4
  • 10
    • 0027641058 scopus 로고
    • The loop problem in proteins: A Monte Carlo simulated annealing approach
    • Carlacci, L., Englander, S.W. The loop problem in proteins: A Monte Carlo simulated annealing approach. Biopolymers, 33:1271-1286, 1993.
    • (1993) Biopolymers , vol.33 , pp. 1271-1286
    • Carlacci, L.1    Englander, S.W.2
  • 12
    • 0001118560 scopus 로고
    • Molecular dynamics for problems in structural biology
    • Brooks, B.R. Molecular dynamics for problems in structural biology. Chem. Scripta 29A:165-169, 1989.
    • (1989) Chem. Scripta , vol.29 A , pp. 165-169
    • Brooks, B.R.1
  • 13
    • 0002770218 scopus 로고
    • Protein folding: Theoretical studies of thermodynamics and dynamics
    • Creighton, T.E. (eds.). New York: W.H. Freeman
    • Karplus, M., Shakhnovich, E. Protein folding: Theoretical studies of thermodynamics and dynamics. In: "Protein Folding." Creighton, T.E. (eds.). New York: W.H. Freeman, 1992:127-198.
    • (1992) Protein Folding , pp. 127-198
    • Karplus, M.1    Shakhnovich, E.2
  • 14
  • 15
    • 0027337481 scopus 로고
    • Simulation of α-helix-coil transition in simplified polyvaline: Equilibrium properties and brownian dynamics
    • Schneller, W., Weaver, D.L. Simulation of α-helix-coil transition in simplified polyvaline: Equilibrium properties and brownian dynamics. Biopolymers 33:1519-1535, 1993.
    • (1993) Biopolymers , vol.33 , pp. 1519-1535
    • Schneller, W.1    Weaver, D.L.2
  • 16
    • 0026205054 scopus 로고
    • A molecular dynamics simulation of equilibrium motions and helix-coil transitions
    • Daggett, V., Kollman, P.A., Kuntz, I.D. A molecular dynamics simulation of equilibrium motions and helix-coil transitions. Biopolymers 31:1115-1134, 1991.
    • (1991) Biopolymers , vol.31 , pp. 1115-1134
    • Daggett, V.1    Kollman, P.A.2    Kuntz, I.D.3
  • 17
    • 0344557043 scopus 로고
    • Molecular dynamics and Monte Carlo simulations favour the α-helical form for alanine-based peptides in water
    • Tirado-Rives, J., Maxwell, D.S., Jorgensen, W.L. Molecular dynamics and Monte Carlo simulations favour the α-helical form for alanine-based peptides in water. J. Am. Chem. Soc. 115:11590-11593, 1993.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 11590-11593
    • Tirado-Rives, J.1    Maxwell, D.S.2    Jorgensen, W.L.3
  • 18
    • 0026525048 scopus 로고
    • Molecular dynamics simulation of helix denaturation
    • Daggett, V., Levitt, M. Molecular dynamics simulation of helix denaturation. J. Mol. Biol. 223:1121-1138, 1992.
    • (1992) J. Mol. Biol. , vol.223 , pp. 1121-1138
    • Daggett, V.1    Levitt, M.2
  • 19
    • 0027219504 scopus 로고
    • Protein unfolding pathways explored through molecular dynamics simulations
    • Daggett, V., Levitt, M. Protein unfolding pathways explored through molecular dynamics simulations. J. Mol. Biol. 232:600-619, 1993.
    • (1993) J. Mol. Biol. , vol.232 , pp. 600-619
    • Daggett, V.1    Levitt, M.2
  • 20
    • 0028200975 scopus 로고
    • Helix folding simulations with various initial conformations
    • Sung, S.S. Helix folding simulations with various initial conformations. Biophys. J. 66:1796-1803, 1994.
    • (1994) Biophys. J. , vol.66 , pp. 1796-1803
    • Sung, S.S.1
  • 21
    • 0028952952 scopus 로고
    • Folding simulation of alanine-based peptides with lysine residues
    • Sung, S.S. Folding simulation of alanine-based peptides with lysine residues. Biophys. J. 68:826-834, 1995.
    • (1995) Biophys. J. , vol.68 , pp. 826-834
    • Sung, S.S.1
  • 22
    • 12044251376 scopus 로고
    • A neutral, water-soluble, α-helical peptide: The effect of ionic strength on the helix-coil equilibrium
    • Scholtz, J.M., York, B.J., Stewart, J.M., Baldwin, R.L. A neutral, water-soluble, α-helical peptide: The effect of ionic strength on the helix-coil equilibrium. J. Am. Chem. Soc. 113:5102-5104, 1991.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5102-5104
    • Scholtz, J.M.1    York, B.J.2    Stewart, J.M.3    Baldwin, R.L.4
  • 24
    • 84988053694 scopus 로고
    • An all atom force field for simulations of proteins and nucleic acids
    • Weiner, S.J., Kollman, P.A., Nguyen, D.T., Case, D.A. An all atom force field for simulations of proteins and nucleic acids. J. Comp. Chem. 7:230-252, 1986.
    • (1986) J. Comp. Chem. , vol.7 , pp. 230-252
    • Weiner, S.J.1    Kollman, P.A.2    Nguyen, D.T.3    Case, D.A.4
  • 25
    • 0020621373 scopus 로고
    • Van der Waals picture of liquids, solids, and phase transitions
    • Chandler, D., Weeks, J.D., Andersen, H.C. Van der Waals picture of liquids, solids, and phase transitions. Science 200:787-794, 1983.
    • (1983) Science , vol.200 , pp. 787-794
    • Chandler, D.1    Weeks, J.D.2    Andersen, H.C.3
  • 26
    • 0004240239 scopus 로고
    • New York: Dover Publications
    • Debye, P. "Polar Molecules." New York: Dover Publications, 1929.
    • (1929) Polar Molecules
    • Debye, P.1
  • 27
    • 84990406847 scopus 로고
    • Dielectric effects in biopolymers: The theory of ionic saturation revisited
    • Hingerty, B.E., Ritchie, R.H., Ferrell, T.L., Turner, J.E. Dielectric effects in biopolymers: The theory of ionic saturation revisited. Biopolymers 24:427-439, 1985.
    • (1985) Biopolymers , vol.24 , pp. 427-439
    • Hingerty, B.E.1    Ritchie, R.H.2    Ferrell, T.L.3    Turner, J.E.4
  • 28
    • 0000777707 scopus 로고
    • Energetic coupling between DNA bending and base pair opening
    • Ramstein, J., Lavery, R. Energetic coupling between DNA bending and base pair opening. Proc. Natl. Acad. Sci. USA 85:7231-7235, 1988.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7231-7235
    • Ramstein, J.1    Lavery, R.2
  • 29
    • 0028166615 scopus 로고
    • Dependence on the dielectric model and pH in a synthetic helical peptide studied by Monte Carlo simulated annealing
    • Okamoto Y. Dependence on the dielectric model and pH in a synthetic helical peptide studied by Monte Carlo simulated annealing. Biopolymers 34:529-539, 1994.
    • (1994) Biopolymers , vol.34 , pp. 529-539
    • Okamoto, Y.1
  • 30
    • 0001730560 scopus 로고
    • The dielectric constant of the solution in the diffuse and helmholtz double layers at a charged interface in aqueous solution
    • Conway, B.E., Bockris, J.O., Ammar, I.A. The dielectric constant of the solution in the diffuse and helmholtz double layers at a charged interface in aqueous solution. Trans. Faraday Soc. 47:756-766, 1951.
    • (1951) Trans. Faraday Soc. , vol.47 , pp. 756-766
    • Conway, B.E.1    Bockris, J.O.2    Ammar, I.A.3
  • 31
    • 0022596727 scopus 로고
    • Solvation energy in protein folding and binding
    • Eisenberg, D., Mclachlan, A.D. Solvation energy in protein folding and binding. Nature 319:199-203, 1986.
    • (1986) Nature , vol.319 , pp. 199-203
    • Eisenberg, D.1    Mclachlan, A.D.2
  • 32
    • 0023338543 scopus 로고
    • Accessible surface areas as a measure of the thermodynamic parameters of hydration of peptides
    • Ooi, T., Oobatake, M., Nemethy, G., Scheraga, H.A. Accessible surface areas as a measure of the thermodynamic parameters of hydration of peptides. Proc. Natl. Acad. Sci. USA 84:3086-3090, 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3086-3090
    • Ooi, T.1    Oobatake, M.2    Nemethy, G.3    Scheraga, H.A.4
  • 33
    • 0000113434 scopus 로고
    • Free energies of hydration of solute molecules. 1. Improvement of the hydration shell model by exact computations of overlapping volumes
    • Kang, Y.K., Nemethy, G., Scheraga, H.A. Free energies of hydration of solute molecules. 1. Improvement of the hydration shell model by exact computations of overlapping volumes. J. Phys. Chem. 91:4105-4109, 1987.
    • (1987) J. Phys. Chem. , vol.91 , pp. 4105-4109
    • Kang, Y.K.1    Nemethy, G.2    Scheraga, H.A.3
  • 34
    • 0027080909 scopus 로고
    • Atomic solvation parameters applied to molecular dynamics of proteins in solution
    • Wesson, L., Eisenberg, D. Atomic solvation parameters applied to molecular dynamics of proteins in solution. Protein Sci. 1:227-235, 1992.
    • (1992) Protein Sci. , vol.1 , pp. 227-235
    • Wesson, L.1    Eisenberg, D.2
  • 35
    • 0027883012 scopus 로고
    • Protein structure prediction with a combined solvation free energy-molecular mechanics force field
    • Schiffer, C.A., Caldwell, J.W., Kollman, P.A., Stroud, R.M. Protein structure prediction with a combined solvation free energy-molecular mechanics force field. Mol. Simulation 10:121-149, 1993.
    • (1993) Mol. Simulation , vol.10 , pp. 121-149
    • Schiffer, C.A.1    Caldwell, J.W.2    Kollman, P.A.3    Stroud, R.M.4
  • 37
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., Doolittle, R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132, 1982.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 38
    • 0026076664 scopus 로고
    • Extracting hydrophobic free energies from experimental data: Relationship to protein folding and theoretical models
    • Sharp, K.A., Nicholls, A., Friedman, R., Honig, B. Extracting hydrophobic free energies from experimental data: Relationship to protein folding and theoretical models. Biochemistry 30:9686-9697, 1991.
    • (1991) Biochemistry , vol.30 , pp. 9686-9697
    • Sharp, K.A.1    Nicholls, A.2    Friedman, R.3    Honig, B.4
  • 39
    • 0000484499 scopus 로고
    • Hydrophobic parameters π of amino-acid side chains from the partitioning of N-acetyl-amino-acid amides
    • Fauchere, J.L., Pliska, V. Hydrophobic parameters π of amino-acid side chains from the partitioning of N-acetyl-amino-acid amides. Eur. J. Med. Chem. Chim. Ther. 18: 369-375, 1983.
    • (1983) Eur. J. Med. Chem. Chim. Ther. , vol.18 , pp. 369-375
    • Fauchere, J.L.1    Pliska, V.2
  • 41
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J.P., Ciccotti, G., Berendsen, H.J.C. Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes. J. Comput. Phys. 23:327-341, 1976.
    • (1976) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 42
    • 84988112508 scopus 로고
    • An efficient newton-like method for molecular mechanics energy minimization of large molecules
    • Ponder, J.W., Richards, F.M. An efficient newton-like method for molecular mechanics energy minimization of large molecules. J. Comput. Chem. 8:1016-1024, 1987.
    • (1987) J. Comput. Chem. , vol.8 , pp. 1016-1024
    • Ponder, J.W.1    Richards, F.M.2
  • 43
    • 84986533794 scopus 로고
    • Algorithms for calculating excluded volume and its derivatives as a function of molecular conformation and their use in energy minimization
    • Kundrot, C.E., Ponder, J.W., Richards, F.M. Algorithms for calculating excluded volume and its derivatives as a function of molecular conformation and their use in energy minimization. J. Comput. Chem. 12:402-409, 1991.
    • (1991) J. Comput. Chem. , vol.12 , pp. 402-409
    • Kundrot, C.E.1    Ponder, J.W.2    Richards, F.M.3
  • 44
    • 0025804130 scopus 로고
    • Large differences in the helix propensities of alanine and glycine
    • Chakrabartty, A., Schellman, J.A., Baldwin, R.L. Large differences in the helix propensities of alanine and glycine. Nature 351:586-588, 1991.
    • (1991) Nature , vol.351 , pp. 586-588
    • Chakrabartty, A.1    Schellman, J.A.2    Baldwin, R.L.3
  • 45
    • 0028222235 scopus 로고
    • Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions
    • Chakrabartty, A., Kortemme, T., Baldwin, R.L. Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions. Protein Sci. 3:843-852, 1994.
    • (1994) Protein Sci. , vol.3 , pp. 843-852
    • Chakrabartty, A.1    Kortemme, T.2    Baldwin, R.L.3
  • 48
    • 0025904730 scopus 로고
    • Defining solution conformations of small linear peptides
    • Dyson, H.J., Wright, P.E. Defining solution conformations of small linear peptides. Annu. Rev. Biophys. Chem. 20: 519-538, 1991.
    • (1991) Annu. Rev. Biophys. Chem. , vol.20 , pp. 519-538
    • Dyson, H.J.1    Wright, P.E.2
  • 49
    • 0027435983 scopus 로고
    • 10-helix in alanine-based peptides: Evidence for a length-dependent structural transition
    • 10-helix in alanine-based peptides: Evidence for a length-dependent structural transition. Biochemistry 32:11957-11962, 1993.
    • (1993) Biochemistry , vol.32 , pp. 11957-11962
    • Fiori, W.R.1    Miik, S.M.2    Millhauser, G.L.3
  • 51
    • 0027219183 scopus 로고
    • Experimental molecular dynamics of an alanine-based helical peptide determined by spin label electron spin resonance
    • Miik, S.M., Casteel, K.M., Millhauser, G.L. Experimental molecular dynamics of an alanine-based helical peptide determined by spin label electron spin resonance. Biochemistry 32:8014-8021, 1993.
    • (1993) Biochemistry , vol.32 , pp. 8014-8021
    • Miik, S.M.1    Casteel, K.M.2    Millhauser, G.L.3
  • 52
    • 0028447414 scopus 로고
    • A single carboxy-terminal arginine determines the amino-terminal helix conformation of an alanine-based peptide
    • Fiori, W.R., Lundberg, K.M., Millhauser, G.L. A single carboxy-terminal arginine determines the amino-terminal helix conformation of an alanine-based peptide. Nature Struct. Biol. 1:374-376, 1994.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 374-376
    • Fiori, W.R.1    Lundberg, K.M.2    Millhauser, G.L.3
  • 53
    • 0027955787 scopus 로고
    • Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins
    • Abagyan, R. Totrov, M. Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins. J. Mol. Biol. 235:983-1002, 1994.
    • (1994) J. Mol. Biol. , vol.235 , pp. 983-1002
    • Abagyan, R.1    Totrov, M.2
  • 54
    • 0016352763 scopus 로고
    • Hydrophobic bonding and accessible surface area in proteins
    • Chothia, C. Hydrophobic bonding and accessible surface area in proteins. Nature 248:338-339, 1974.
    • (1974) Nature , vol.248 , pp. 338-339
    • Chothia, C.1
  • 55
    • 0024290488 scopus 로고
    • Helix signals in proteins
    • Presta, L.P., Rose, G.D. Helix signals in proteins. Science 240:1632-1641, 1988.
    • (1988) Science , vol.240 , pp. 1632-1641
    • Presta, L.P.1    Rose, G.D.2
  • 56
    • 0025877673 scopus 로고
    • Prediction of the thermodynamics of protein unfolding: The helix coil transition of poly(L-alanine)
    • Ooi, T., Oobatake, M. Prediction of the thermodynamics of protein unfolding: The helix coil transition of poly(L-alanine). Proc. Natl. Acad. Sci. USA 88:2859-2863, 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2859-2863
    • Ooi, T.1    Oobatake, M.2
  • 58
    • 0027497118 scopus 로고
    • The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide
    • Seholtz, J.M., Qian, H., Robbina, V.H., Baldwin, R.L. The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide. Biochemistry 32:9668-9676, 1993.
    • (1993) Biochemistry , vol.32 , pp. 9668-9676
    • Seholtz, J.M.1    Qian, H.2    Robbina, V.H.3    Baldwin, R.L.4
  • 59
    • 33947476272 scopus 로고
    • The factors affecting the stability of hydrogen-bonded polypeptide structures in solution
    • Schellman, J.A. The factors affecting the stability of hydrogen-bonded polypeptide structures in solution. J. Phys. Chem. 62:1485-1494, 1958.
    • (1958) J. Phys. Chem. , vol.62 , pp. 1485-1494
    • Schellman, J.A.1
  • 60
    • 0000668407 scopus 로고
    • Theory of the phase transition between helix and random coil in polypeptide chains
    • Zimm, B.H., Bragg, J.K. Theory of the phase transition between helix and random coil in polypeptide chains. J. Chem. Phys. 31:526-535, 1959.
    • (1959) J. Chem. Phys. , vol.31 , pp. 526-535
    • Zimm, B.H.1    Bragg, J.K.2
  • 61
    • 0000333671 scopus 로고
    • On the theory of helix-coil transition in polypeptides
    • Lifson, S., Roig, A. On the theory of helix-coil transition in polypeptides. J. Chem. Phys. 34:1963-1974, 1961.
    • (1961) J. Chem. Phys. , vol.34 , pp. 1963-1974
    • Lifson, S.1    Roig, A.2
  • 63
    • 33751391161 scopus 로고
    • Helix-coil theories: A comparative study for finite length polypeptides
    • Qian, H., Schellman, J.A. Helix-coil theories: A comparative study for finite length polypeptides. J. Phys. Chem. 96:3987-3994, 1992.
    • (1992) J. Phys. Chem. , vol.96 , pp. 3987-3994
    • Qian, H.1    Schellman, J.A.2
  • 64
    • 0026773206 scopus 로고
    • The mechanism of α-helix formation by peptides
    • Scholtz, J.M., Baldwin, R.L. The mechanism of α-helix formation by peptides. Annu. Rev. Biomol. Struct. 21:95-118, 1992.
    • (1992) Annu. Rev. Biomol. Struct , vol.21 , pp. 95-118
    • Scholtz, J.M.1    Baldwin, R.L.2
  • 65
    • 84924719416 scopus 로고
    • On the dominance of short-range interactions in polypeptides and proteins
    • Scheraga, H.A. On the dominance of short-range interactions in polypeptides and proteins. Pure Appl. Chem. 36: 1-8, 1973.
    • (1973) Pure Appl. Chem. , vol.36 , pp. 1-8
    • Scheraga, H.A.1
  • 68
    • 0028947257 scopus 로고
    • Funnels, pathways, and energy landscape of protein folding: A synthesis
    • Bryngelson, J.D., Onuchic, J.N., Socci, N.D., Wolynes, P.G. Funnels, pathways, and energy landscape of protein folding: A synthesis. Proteins 21:167-195, 1995.
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 69
    • 0015914742 scopus 로고
    • Structural and functional role of leucine residues in proteins
    • Chou, P.Y., Fasman, G.D. Structural and functional role of leucine residues in proteins. J. Mol. Biol. 74:263-281, 1973.
    • (1973) J. Mol. Biol. , vol.74 , pp. 263-281
    • Chou, P.Y.1    Fasman, G.D.2
  • 70
    • 0000824554 scopus 로고
    • Helix-coil stability constants for the naturally occurring amino acids in water. 22. Histidine parameters from random poly[(hydroxybutyl)glutamine-co-histidine]
    • Sueki, M., Lee, S., Powers, S.P., Denton, J.B., Konishi, Y., Scheraga, H.A. Helix-coil stability constants for the naturally occurring amino acids in water. 22. Histidine parameters from random poly[(hydroxybutyl)glutamine-co-histidine]. Macromolecules. 17:148-155, 1984.
    • (1984) Macromolecules , vol.17 , pp. 148-155
    • Sueki, M.1    Lee, S.2    Powers, S.P.3    Denton, J.B.4    Konishi, Y.5    Scheraga, H.A.6
  • 71
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acides
    • O'Neil, K.T., DeGrado, W.F. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acides. Science 250:646-651, 1990.
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 72
    • 0025260032 scopus 로고
    • Side chain contribution to the stability of alpha-helical structure in peptides
    • Lyu, P.C., Liff, M.I., Marky, L.A., Kallenbach, N.R. Side chain contribution to the stability of alpha-helical structure in peptides. Science 250:669-673, 1990.
    • (1990) Science , vol.250 , pp. 669-673
    • Lyu, P.C.1    Liff, M.I.2    Marky, L.A.3    Kallenbach, N.R.4
  • 73
    • 0028359608 scopus 로고
    • Helix-forming tendencies of nonpolar amino acids predicted by Monte Carlo simulated annealing
    • Okamoto, Y. Helix-forming tendencies of nonpolar amino acids predicted by Monte Carlo simulated annealing. Proteins 19:14-23, 1994.
    • (1994) Proteins , vol.19 , pp. 14-23
    • Okamoto, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.