메뉴 건너뛰기




Volumn 270, Issue 2, 1997, Pages 305-317

Thermodynamics of a reverse turn motif. Solvent effects and side-chain packing

Author keywords

Electrostatics; Folding; Peptide; Poisson Boltzmann equation; Solvation free energy

Indexed keywords

PENTAPEPTIDE; SOLVENT;

EID: 0030852818     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1103     Document Type: Article
Times cited : (35)

References (64)
  • 1
    • 0028883794 scopus 로고
    • Determination of the conformation of folding initiation sites in proteins by computer simulation
    • Avbelj F., Moult J. Determination of the conformation of folding initiation sites in proteins by computer simulation. Proteins: Struct. Funct. Genet. 23:1995;129-141.
    • (1995) Proteins: Struct. Funct. Genet. , vol.23 , pp. 129-141
    • Avbelj, F.1    Moult, J.2
  • 2
    • 33751499830 scopus 로고
    • Multiple-site titration curves of proteins: An analysis of exact and approximate methods for their calculation
    • Bashford D., Karplus M. Multiple-site titration curves of proteins: an analysis of exact and approximate methods for their calculation. J. Phys. Chem. 95:1991;9556-9561.
    • (1991) J. Phys. Chem. , vol.95 , pp. 9556-9561
    • Bashford, D.1    Karplus, M.2
  • 4
    • 0030953142 scopus 로고    scopus 로고
    • A computational study of the role of solvation effects in reverse turn formation in the tetrapeptides APGD and APGN
    • Bashford D., Case D. A., Choi C., Gippert G. P. A computational study of the role of solvation effects in reverse turn formation in the tetrapeptides APGD and APGN. J. Am. Chem. Soc. 119:1997;4964-4971.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 4964-4971
    • Bashford, D.1    Case, D.A.2    Choi, C.3    Gippert, G.P.4
  • 5
    • 0024578173 scopus 로고
    • Free energy via molecular simulation: Applications to chemical and biomolecular systems
    • Beveridge D., DiCapua F. M. Free energy via molecular simulation: applications to chemical and biomolecular systems. Annu. Rev. Biophys. Biophys. Chem. 18:1989;431-492.
    • (1989) Annu. Rev. Biophys. Biophys. Chem. , vol.18 , pp. 431-492
    • Beveridge, D.1    DiCapua, F.M.2
  • 6
    • 34250928962 scopus 로고
    • Volumes and heats of hydration of ions
    • Born M. Volumes and heats of hydration of ions. Z. Phys. 1:1920;45-48.
    • (1920) Z. Phys. , vol.1 , pp. 45-48
    • Born, M.1
  • 7
    • 0342348575 scopus 로고
    • Conformational distribution of a tetrapeptide in solution using a combined random search and continuum dielectric approach
    • Chan S. L., Lim C. Conformational distribution of a tetrapeptide in solution using a combined random search and continuum dielectric approach. J. Phys. Chem. 98:1994;12805-12814.
    • (1994) J. Phys. Chem. , vol.98 , pp. 12805-12814
    • Chan, S.L.1    Lim, C.2
  • 8
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly M. L. Solvent-accessible surfaces of proteins and nucleic acids. Science. 221:1983;709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 9
    • 84962464697 scopus 로고    scopus 로고
    • Quantum mechanical geometry optimization in solution using a finite element continuum electrostatics method
    • Cortis C. M., Langlois J.-M., Beachy M. D., Friesner R. A. Quantum mechanical geometry optimization in solution using a finite element continuum electrostatics method. J. Chem. Phys. 105:1996;5472-5484.
    • (1996) J. Chem. Phys. , vol.105 , pp. 5472-5484
    • Cortis, C.M.1    Langlois, J.-M.2    Beachy, M.D.3    Friesner, R.A.4
  • 12
    • 0030627746 scopus 로고    scopus 로고
    • Dynamics of a type VI turn in a linear peptide in aqueous solution
    • Demchuk E., Bashford D., Case D. A. Dynamics of a type VI turn in a linear peptide in aqueous solution. Folding Des. 2:1997;35-46.
    • (1997) Folding Des. , vol.2 , pp. 35-46
    • Demchuk, E.1    Bashford, D.2    Case, D.A.3
  • 13
    • 0028053187 scopus 로고
    • Understanding how proteins fold: The lysozyme story so far
    • Dobson C. M., Evans P., Radford S. E. Understanding how proteins fold: the lysozyme story so far. Trends Biochem. Sci. 19:1994;31-37.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 31-37
    • Dobson, C.M.1    Evans, P.2    Radford, S.E.3
  • 14
    • 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. Biophys. Chem. 20:1991;519-538.
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 519-538
    • Dyson, H.J.1    Wright, P.E.2
  • 15
    • 0024278597 scopus 로고
    • Folding of immunogenic peptide fragments of proteins in water solution. I. Sequence requirements for the formation of reverse turn
    • Dyson H. J., Rance M., Houghten R. A., Lerner R. A., Wright P. Folding of immunogenic peptide fragments of proteins in water solution. I. Sequence requirements for the formation of reverse turn. J. Mol. Biol. 201:1988a;161-200.
    • (1988) J. Mol. Biol. , vol.201 , pp. 161-200
    • Dyson, H.J.1    Rance, M.2    Houghten, R.A.3    Lerner, R.A.4    Wright, P.5
  • 16
    • 0023803794 scopus 로고
    • The physical basis for induction of protein-reactive antipeptide antibodies
    • Dyson H. J., Lerner R. A., Wright P. E. The physical basis for induction of protein-reactive antipeptide antibodies. Annu. Rev. Biophys. Biophys. Chem. 17:1988b;305-324.
    • (1988) Annu. Rev. Biophys. Biophys. Chem. , vol.17 , pp. 305-324
    • Dyson, H.J.1    Lerner, R.A.2    Wright, P.E.3
  • 17
    • 0026768829 scopus 로고
    • Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin
    • Dyson H. J., Merutka G., Waltho J. P., Lerner R. A., Wright P. E. Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin. J. Mol. Biol. 226:1992a;795-817.
    • (1992) J. Mol. Biol. , vol.226 , pp. 795-817
    • Dyson, H.J.1    Merutka, G.2    Waltho, J.P.3    Lerner, R.A.4    Wright, P.E.5
  • 18
    • 0026743136 scopus 로고
    • Folding of peptide fragments comprising the complete sequence of proteins, models for initiation of protein folding. II. Plastocyanin
    • Dyson H. J., Sayre J. R., Merutka G., Shin H.-C., Lerner R. A., Wright P. Folding of peptide fragments comprising the complete sequence of proteins, models for initiation of protein folding. II. Plastocyanin. J. Mol. Biol. 226:1992b;819-835.
    • (1992) J. Mol. Biol. , vol.226 , pp. 819-835
    • Dyson, H.J.1    Sayre, J.R.2    Merutka, G.3    Shin, H.-C.4    Lerner, R.A.5    Wright, P.6
  • 19
    • 0022596727 scopus 로고
    • Solvation energy in protein folding and binding
    • Eisenberg D., McLachlan A. D. Solvation energy in protein folding and binding. Nature. 319:1986;199-203.
    • (1986) Nature , vol.319 , pp. 199-203
    • Eisenberg, D.1    McLachlan, A.D.2
  • 20
    • 84913591509 scopus 로고
    • Improved strategy in analytic surface calculation for molecular systems: Handling of singularities and computational efficiency
    • Eisenhaber F., Argos P. Improved strategy in analytic surface calculation for molecular systems: handling of singularities and computational efficiency. J. Comput. Chem. 14:1993;272-1280.
    • (1993) J. Comput. Chem. , vol.14 , pp. 272-1280
    • Eisenhaber, F.1    Argos, P.2
  • 21
    • 0027163998 scopus 로고
    • Protein folding and stability: The pathway of folding of barnase
    • Fersht A. R. Protein folding and stability: the pathway of folding of barnase. FEBS Letters. 325:1993;5-16.
    • (1993) FEBS Letters , vol.325 , pp. 5-16
    • Fersht, A.R.1
  • 22
    • 84986439462 scopus 로고
    • Molecular dynamics simulation with a continuum electrostatic model of the solvent
    • Gilson M. K., McCammon J. A., Madura J. D. Molecular dynamics simulation with a continuum electrostatic model of the solvent. J. Comput. Chem. 16:1995;1080-1095.
    • (1995) J. Comput. Chem. , vol.16 , pp. 1080-1095
    • Gilson, M.K.1    McCammon, J.A.2    Madura, J.D.3
  • 24
    • 0011930746 scopus 로고
    • Theory of hydrophobic bonding. II. The correlation of hydrocarbon solubility in water with solvent cavity surface area
    • Hermann R. B. Theory of hydrophobic bonding. II. The correlation of hydrocarbon solubility in water with solvent cavity surface area. J. Phys. Chem. 76:1972;2754-2759.
    • (1972) J. Phys. Chem. , vol.76 , pp. 2754-2759
    • Hermann, R.B.1
  • 25
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig B., Nicholls A. Classical electrostatics in biology and chemistry. Science. 268:1995;1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 26
    • 33751385054 scopus 로고
    • Macroscopic models of aqueous solutions: Biological and chemical applications
    • Honig B., Sharp K., Yang A.-S. Macroscopic models of aqueous solutions: biological and chemical applications. J. Phys. Chem. 97:1993;1101-1109.
    • (1993) J. Phys. Chem. , vol.97 , pp. 1101-1109
    • Honig, B.1    Sharp, K.2    Yang, A.-S.3
  • 27
    • 0016548979 scopus 로고
    • Investigation of the conformations of four tetrapeptides by nuclear magnetic resonance and circular dichroism spectroscopy, and conformational energy calculations
    • Howard J. C., Ali A., Scheraga H. A., Momany F. A. Investigation of the conformations of four tetrapeptides by nuclear magnetic resonance and circular dichroism spectroscopy, and conformational energy calculations. Macromolecules. 8:1975;607-622.
    • (1975) Macromolecules , vol.8 , pp. 607-622
    • Howard, J.C.1    Ali, A.2    Scheraga, H.A.3    Momany, F.A.4
  • 28
    • 0000299809 scopus 로고
    • Aromatic-aromatic interactions: Free energy profiles for the benzene dimer in water, chloroform, and liquid benzene
    • Jorgensen W. L., Severance D. L. Aromatic-aromatic interactions: free energy profiles for the benzene dimer in water, chloroform, and liquid benzene. J. Am. Chem. Soc. 112:1990;4768-4774.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 4768-4774
    • Jorgensen, W.L.1    Severance, D.L.2
  • 29
    • 33645941402 scopus 로고
    • The OPLS potential functions for proteins. Energy minimization for crystals of cyclic peptides and crambin
    • Jorgensen W. L., Tirado-Rives J. The OPLS potential functions for proteins. Energy minimization for crystals of cyclic peptides and crambin. J. Am. Chem. Soc. 110:1988;1657-1666.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 30
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim P. S., Baldwin R. L. Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 51:1982;459-489.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 31
    • 36449009704 scopus 로고
    • Reaction paths and free energy profiles for conformational transitions: An internal coordinate approach
    • Lazaridis T., Tobias D. J., Brooks C. L., III, Paulaitis M. E. Reaction paths and free energy profiles for conformational transitions: an internal coordinate approach. J. Chem. Phys. 95:1991;7612-7625.
    • (1991) J. Chem. Phys. , vol.95 , pp. 7612-7625
    • Lazaridis, T.1    Tobias, D.J.2    Brooks C.L. III3    Paulaitis, M.E.4
  • 32
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B., Richards F. M. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55:1971;379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 34
    • 0030001915 scopus 로고    scopus 로고
    • On the entropy of protein folding
    • Makhatadze G. I., Privalov P. L. On the entropy of protein folding. Protein Sci. 5:1996;507-510.
    • (1996) Protein Sci. , vol.5 , pp. 507-510
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 35
    • 0000435390 scopus 로고    scopus 로고
    • Comparison of continuum and explicit models of solvation: Potentials of mean force for alanine dipeptide
    • Marrone T. J., Gilson M. K., McCammon A. J. Comparison of continuum and explicit models of solvation: potentials of mean force for alanine dipeptide. J. Chem. Phys. 100:1996;1439-1441.
    • (1996) J. Chem. Phys. , vol.100 , pp. 1439-1441
    • Marrone, T.J.1    Gilson, M.K.2    McCammon, A.J.3
  • 36
    • 0023338543 scopus 로고
    • Accessible surface areas as a measure of the thermodynamic parameters of hydration of peptides
    • Ooi T., Oobatake M., Nemthy G., Scheraga H. A. Accessible surface areas as a measure of the thermodynamic parameters of hydration of peptides. Proc. Natl Acad. Sci. USA. 84:1987;3086-3090.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3086-3090
    • Ooi, T.1    Oobatake, M.2    Nemthy, G.3    Scheraga, H.A.4
  • 37
    • 0001611806 scopus 로고    scopus 로고
    • Dielectric continuum models for hydration effects on peptide conformational transitions
    • Ösapay K., Young W. S., Bashford D., Brooks C. L., III, Case D. A. Dielectric continuum models for hydration effects on peptide conformational transitions. J. Phys. Chem. 100:1996;2698-2705.
    • (1996) J. Phys. Chem. , vol.100 , pp. 2698-2705
    • Ösapay, K.1    Young, W.S.2    Bashford, D.3    Brooks C.L. III4    Case, D.A.5
  • 38
    • 0017429069 scopus 로고
    • Areas, volumes, packing and protein structure
    • Richards F. M. Areas, volumes, packing and protein structure. Annu. Rev. Biophys. Bioeng. 6:1977;151-176.
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 39
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson J. S. The anatomy and taxonomy of protein structure. Advan. Protein Chem. 34:1981;167-339.
    • (1981) Advan. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 40
    • 0028157226 scopus 로고
    • Backbone flexibility and stability of reverse turn conformation in a model system
    • Scully J., Hermans J. Backbone flexibility and stability of reverse turn conformation in a model system. J. Mol. Biol. 235:1994;682-694.
    • (1994) J. Mol. Biol. , vol.235 , pp. 682-694
    • Scully, J.1    Hermans, J.2
  • 41
    • 84986430566 scopus 로고
    • Incorporating solvent and ion screening into molecular dynamics using the finite-difference Poisson-Boltzmann method
    • Sharp K. A. Incorporating solvent and ion screening into molecular dynamics using the finite-difference Poisson-Boltzmann method. J. Comput. Chem. 12:1991;454-468.
    • (1991) J. Comput. Chem. , vol.12 , pp. 454-468
    • Sharp, K.A.1
  • 42
    • 0000831520 scopus 로고
    • Solvation free energies estimated from macroscopic continuum theory: An accuracy assessment
    • Simonson T., Brünger A. T. Solvation free energies estimated from macroscopic continuum theory: an accuracy assessment. J. Phys. Chem. 98:1994;4683-4694.
    • (1994) J. Phys. Chem. , vol.98 , pp. 4683-4694
    • Simonson, T.1    Brünger, A.T.2
  • 43
    • 32844457567 scopus 로고
    • Accurate calculation of hydration free energies using macroscopic solvent models
    • Sitkoff D., Sharp K. A., Honig B. Accurate calculation of hydration free energies using macroscopic solvent models. J. Phys. Chem. 98:1994;1978-1988.
    • (1994) J. Phys. Chem. , vol.98 , pp. 1978-1988
    • Sitkoff, D.1    Sharp, K.A.2    Honig, B.3
  • 44
    • 0028040064 scopus 로고
    • Evaluation of the conformational free energies of loops in proteins
    • Smith K. C., Honig B. Evaluation of the conformational free energies of loops in proteins. Proteins: Struct. Funct. Genet. 18:1994;119-132.
    • (1994) Proteins: Struct. Funct. Genet. , vol.18 , pp. 119-132
    • Smith, K.C.1    Honig, B.2
  • 45
    • 0024975174 scopus 로고
    • Thermodynamics of amide hydrogen bond formation in polar and apolar solvents
    • Sneddon S. F., Tobias D. J., Brooks C. L., III. Thermodynamics of amide hydrogen bond formation in polar and apolar solvents. J. Mol. Biol. 209:1989;817-820.
    • (1989) J. Mol. Biol. , vol.209 , pp. 817-820
    • Sneddon, S.F.1    Tobias, D.J.2    Brooks C.L. III3
  • 46
    • 0000328844 scopus 로고
    • A new vertex algorithm to calculate solvent accessible surface areas
    • Sridharan S., Nicholls A., Honig B. A new vertex algorithm to calculate solvent accessible surface areas. Biophys. J. 61:1992;A174.
    • (1992) Biophys. J. , vol.61
    • Sridharan, S.1    Nicholls, A.2    Honig, B.3
  • 47
    • 0344778061 scopus 로고
    • Semianalytical treatment of solvation for molecular mechanics and dynamics
    • Still W. C., Tempczyk A., Hawley R. C., Hendrickson T. Semianalytical treatment of solvation for molecular mechanics and dynamics. J. Am. Chem. Soc. 112:1990;6127-6129.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 6127-6129
    • Still, W.C.1    Tempczyk, A.2    Hawley, R.C.3    Hendrickson, T.4
  • 48
    • 0025679019 scopus 로고
    • Reverse turns in blocked dipeptides are intrinsically unstable in water
    • Tobias D. J., Sneddon S. F., Brooks C. L., III. Reverse turns in blocked dipeptides are intrinsically unstable in water. J. Mol. Biol. 216:1991a;783-796.
    • (1991) J. Mol. Biol. , vol.216 , pp. 783-796
    • Tobias, D.J.1    Sneddon, S.F.2    Brooks C.L. III3
  • 49
    • 0000055779 scopus 로고
    • The stability of protein secondary structures in aqueous solution
    • Obernai, France: American Institute of Physics
    • Tobias D. J., Sneddon S. F., Brooks C. L., III. The stability of protein secondary structures in aqueous solution. Advances in Biomolecular Simulations. 1991b;American Institute of Physics, Obernai, France.
    • (1991) Advances in Biomolecular Simulations
    • Tobias, D.J.1    Sneddon, S.F.2    Brooks C.L. III3
  • 50
    • 11744256643 scopus 로고
    • Molecular interactions in solution: An overview of methods based on continuous distributions of solvent
    • Tomasi J., Persico M. Molecular interactions in solution: an overview of methods based on continuous distributions of solvent. Chem. Rev. 94:1994;2027-2094.
    • (1994) Chem. Rev. , vol.94 , pp. 2027-2094
    • Tomasi, J.1    Persico, M.2
  • 51
    • 0026076082 scopus 로고
    • Empirical solvation models can be used to differentiate native from near-native conformations of bovine pancreatic trypsin inhibitor
    • Vila J., Williams R. L., Vasquez M., Scheraga H. A. Empirical solvation models can be used to differentiate native from near-native conformations of bovine pancreatic trypsin inhibitor. Proteins: Struct. Funct. Genet. 10:1991;199-218.
    • (1991) Proteins: Struct. Funct. Genet. , vol.10 , pp. 199-218
    • Vila, J.1    Williams, R.L.2    Vasquez, M.3    Scheraga, H.A.4
  • 52
    • 0027165688 scopus 로고
    • Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin
    • Waltho J. P., Feher V. A., Merutka G., Dyson H. J., Wright P. E. Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin. Biochemistry. 32:1993;6337-6347.
    • (1993) Biochemistry , vol.32 , pp. 6337-6347
    • Waltho, J.P.1    Feher, V.A.2    Merutka, G.3    Dyson, H.J.4    Wright, P.E.5
  • 53
    • 0030271002 scopus 로고    scopus 로고
    • Energetic decomposition of the α-helix-coil equilibrium of a dynamic model system
    • Wang L., O'Connell T., Tropsha A., Hermans J. Energetic decomposition of the α-helix-coil equilibrium of a dynamic model system. Biopolymers. 39:1996;479-489.
    • (1996) Biopolymers , vol.39 , pp. 479-489
    • Wang, L.1    O'Connell, T.2    Tropsha, A.3    Hermans, J.4
  • 54
    • 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. Comput. Chem. 7:1986;230-252.
    • (1986) J. Comput. Chem. , vol.7 , pp. 230-252
    • Weiner, S.J.1    Kollman, P.A.2    Nguyen, D.T.3    Case, D.A.4
  • 55
    • 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. 1:1992;227-235.
    • (1992) Protein Sci. , vol.1 , pp. 227-235
    • Wesson, L.1    Eisenberg, D.2
  • 56
    • 0025113022 scopus 로고
    • β-turns and their distortions: A proposed new nomenclature
    • Wilmot C. M., Thornton J. M. β-Turns and their distortions: a proposed new nomenclature. Protein Eng. 3:1990;479-493.
    • (1990) Protein Eng. , vol.3 , pp. 479-493
    • Wilmot, C.M.1    Thornton, J.M.2
  • 57
    • 0024293204 scopus 로고
    • Conformation of peptide fragments of proteins in aqueous solution: Implications for initiation of protein folding
    • Wright P. E., Dyson H. J., Lerner R. A. Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding. Biochemistry. 27:1988;7167-7175.
    • (1988) Biochemistry , vol.27 , pp. 7167-7175
    • Wright, P.E.1    Dyson, H.J.2    Lerner, R.A.3
  • 58
    • 0029121068 scopus 로고
    • Free energy determinants of secondary structure formation. I. α-Helices
    • Yang A.-S., Honig B. Free energy determinants of secondary structure formation. I. α-Helices. J. Mol. Biol. 252:1995a;351-365.
    • (1995) J. Mol. Biol. , vol.252 , pp. 351-365
    • Yang, A.-S.1    Honig, B.2
  • 59
    • 0029150955 scopus 로고
    • Free energy determinants of secondary structure formation. II. Antiparallel β-sheets
    • Yang A.-S., Honig B. Free energy determinants of secondary structure formation. II. Antiparallel β-sheets. J. Mol. Biol. 252:1995b;366-376.
    • (1995) J. Mol. Biol. , vol.252 , pp. 366-376
    • Yang, A.-S.1    Honig, B.2
  • 60
    • 0030596522 scopus 로고    scopus 로고
    • Free energy determinants of secondary structure formation. III. β-Turns and their role in protein folding
    • Yang A.-S., Hitz B., Honig B. Free energy determinants of secondary structure formation. III. β-Turns and their role in protein folding. J. Mol. Biol. 259:1996;873-882.
    • (1996) J. Mol. Biol. , vol.259 , pp. 873-882
    • Yang, A.-S.1    Hitz, B.2    Honig, B.3
  • 62
    • 0028068045 scopus 로고
    • Three-dimensional structure of a type VI turn in a linear peptide in water solution. Evidence for stacking of aromatic rings as a major stabilizing factor
    • Yao J., Dyson H. J., Wright P. E. Three-dimensional structure of a type VI turn in a linear peptide in water solution. Evidence for stacking of aromatic rings as a major stabilizing factor. J. Mol. Biol. 243:1994a;736-753.
    • (1994) J. Mol. Biol. , vol.243 , pp. 736-753
    • Yao, J.1    Dyson, H.J.2    Wright, P.E.3
  • 63
    • 0028068045 scopus 로고
    • Stabilization of a type VI turn in a family of linear peptides in water solution
    • Yao J., Feher V. A., Espejo B. F., Reymond M. T., Wright P. E., Dyson H. J. Stabilization of a type VI turn in a family of linear peptides in water solution. J. Mol. Biol. 243:1994b;754-766.
    • (1994) J. Mol. Biol. , vol.243 , pp. 754-766
    • Yao, J.1    Feher, V.A.2    Espejo, B.F.3    Reymond, M.T.4    Wright, P.E.5    Dyson, H.J.6
  • 64
    • 84986431462 scopus 로고
    • An analytical algorithm for the rapid determination of the solvent accessibility of points in a three-dimensional lattice around a solute molecule
    • You T., Bashford D. An analytical algorithm for the rapid determination of the solvent accessibility of points in a three-dimensional lattice around a solute molecule. J. Comput. Chem. 16:1995;743-757.
    • (1995) J. Comput. Chem. , vol.16 , pp. 743-757
    • You, T.1    Bashford, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.