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Volumn 44, Issue 28, 2005, Pages 9691-9702

Helix, sheet, and polyproline II frequencies and strong nearest neighbor effects in a restricted coil library

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOPOLYMERS; MASKS; POLYPROPYLENES; PROBABILITY DENSITY FUNCTION; SOLVENT EXTRACTION; TRAVELING WAVE TUBES;

EID: 22244458915     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0474822     Document Type: Article
Times cited : (157)

References (63)
  • 1
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal, C. (1968) Are there pathways for protein folding? J. Chem. Phys. 65, 44-45.
    • (1968) J. Chem. Phys. , vol.65 , pp. 44-45
    • Levinthal, C.1
  • 4
    • 84987322752 scopus 로고
    • The circular dichroism spectrum and structure of unordered polypeptides and proteins
    • Krimm, S., and Tiffany, M. L. (1974) The circular dichroism spectrum and structure of unordered polypeptides and proteins, Isr. J. Chem. 12, 189-200.
    • (1974) Isr. J. Chem. , vol.12 , pp. 189-200
    • Krimm, S.1    Tiffany, M.L.2
  • 5
    • 0042701995 scopus 로고    scopus 로고
    • Investigations into sequence and conformational dependence of backbone entropy, inter-basin dynamics and the Flory isolated-pair hypothesis for peptides
    • Zaman, M. H., Shen, M. Y., Berry, R. S., Freed, K. F., and Sosnick, T. R. (2003) Investigations into sequence and conformational dependence of backbone entropy, inter-basin dynamics and the Flory isolated-pair hypothesis for peptides, J. Mol. Biol. 331, 693-711.
    • (2003) J. Mol. Biol. , vol.331 , pp. 693-711
    • Zaman, M.H.1    Shen, M.Y.2    Berry, R.S.3    Freed, K.F.4    Sosnick, T.R.5
  • 6
    • 0033730431 scopus 로고    scopus 로고
    • The Flory isolated-pair hypothesis is not valid for polypeptide chains: Implications for protein folding
    • Pappu, R. V., Srinivasan, R., and Rose, G. D. (2000) The Flory isolated-pair hypothesis is not valid for polypeptide chains: implications for protein folding, Proc. Natl. Acad. Sci., U.S.A. 97, 12565-12570.
    • (2000) Proc. Natl. Acad. Sci., U.S.A. , vol.97 , pp. 12565-12570
    • Pappu, R.V.1    Srinivasan, R.2    Rose, G.D.3
  • 7
    • 0029978353 scopus 로고    scopus 로고
    • Analysis of main chain torsion angles in proteins: Prediction of NMR coupling constants for native and random coil conformations
    • Smith, L. J., Bolin, K. A., Schwalbe, H., MacArthur, M. W., Thornton, J. M., and Dobson, C. M. (1996) Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations, J. Mol. Biol. 255, 494-506.
    • (1996) J. Mol. Biol. , vol.255 , pp. 494-506
    • Smith, L.J.1    Bolin, K.A.2    Schwalbe, H.3    MacArthur, M.W.4    Thornton, J.M.5    Dobson, C.M.6
  • 8
    • 2542560465 scopus 로고    scopus 로고
    • Relationships between amino acid sequence and backbone torsion angle preferences
    • Keskin, O., Yuret, D., Gursoy, A., Turkay, M., and Erman, B. (2004) Relationships between amino acid sequence and backbone torsion angle preferences, Proteins 55, 992-998.
    • (2004) Proteins , vol.55 , pp. 992-998
    • Keskin, O.1    Yuret, D.2    Gursoy, A.3    Turkay, M.4    Erman, B.5
  • 10
    • 0023555768 scopus 로고
    • Further developments of protein secondary structure prediction using information theory. New parameters and consideration of residue pairs
    • Gibrat, J. F., Garnier, J., and Robson, B. (1987) Further developments of protein secondary structure prediction using information theory. New parameters and consideration of residue pairs, J. Mol. Biol. 198, 425-443.
    • (1987) J. Mol. Biol. , vol.198 , pp. 425-443
    • Gibrat, J.F.1    Garnier, J.2    Robson, B.3
  • 11
    • 0027407722 scopus 로고
    • Estimation and use of protein backbone angle probabilities
    • Kang, H. S., Kurochkina, N. A., and Lee, B. (1993) Estimation and use of protein backbone angle probabilities, J. Mol. Biol. 229, 448-460.
    • (1993) J. Mol. Biol. , vol.229 , pp. 448-460
    • Kang, H.S.1    Kurochkina, N.A.2    Lee, B.3
  • 13
    • 0037456294 scopus 로고    scopus 로고
    • Computer simulation of met-enkephalin using explicit atom and united atom potentials: Similarities, differences, and suggestions for improvement
    • Zaman, M. H., Shen, M. Y., Berry, R. S., and Freed, K. F. (2003) Computer simulation of met-enkephalin using explicit atom and united atom potentials: Similarities, differences, and suggestions for improvement, J. Phys. Chem. B 107, 1685-1691.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 1685-1691
    • Zaman, M.H.1    Shen, M.Y.2    Berry, R.S.3    Freed, K.F.4
  • 14
    • 0038241788 scopus 로고    scopus 로고
    • Conformational dynamics of trialanine in water. 2. Comparison of AMBER, CHARMM, GROMOS, and OPLS force fields to NMR and infrared experiments
    • Mu, Y. G., Kosov, D. S., and Stock, G. (2003) Conformational dynamics of trialanine in water. 2. Comparison of AMBER, CHARMM, GROMOS, and OPLS force fields to NMR and infrared experiments, J. Phys. Chem. B 107, 5064-5073.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 5064-5073
    • Mu, Y.G.1    Kosov, D.S.2    Stock, G.3
  • 15
    • 0037441479 scopus 로고    scopus 로고
    • Comparison of a QM/MM force field and molecular mechanics force fields in simulations of alanine and glycine "dipeptides" (Ace-Ala-Nme and Ace-Gly-Nme) in water in relation to the problem of modeling the unfolded peptide backbone in solution
    • Hu, H., Elstner, M., and Hermans, J. (2003) Comparison of a QM/ MM force field and molecular mechanics force fields in simulations of alanine and glycine "dipeptides" (Ace-Ala-Nme and Ace-Gly-Nme) in water in relation to the problem of modeling the unfolded peptide backbone in solution, Proteins 50, 451-463.
    • (2003) Proteins , vol.50 , pp. 451-463
    • Hu, H.1    Elstner, M.2    Hermans, J.3
  • 16
    • 0037022662 scopus 로고    scopus 로고
    • Alpha-helical stabilization by side chain shielding of backbone hydrogen bonds
    • Garcia, A. E., and Sanbonmatsu, K. Y. (2002) Alpha-helical stabilization by side chain shielding of backbone hydrogen bonds. Proc. Natl. Acad. Sci., U.S.A. 99, 2782-2787.
    • (2002) Proc. Natl. Acad. Sci., U.S.A. , vol.99 , pp. 2782-2787
    • Garcia, A.E.1    Sanbonmatsu, K.Y.2
  • 17
    • 0028568650 scopus 로고
    • Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrixes: Comparison with experimental scales
    • Munoz, V., and Serrano, L. (1994) Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrixes: comparison with experimental scales, Proteins 20, 301-311.
    • (1994) Proteins , vol.20 , pp. 301-311
    • Munoz, V.1    Serrano, L.2
  • 18
    • 0029147823 scopus 로고
    • Intrinsic phi, psi propensities of amino acids, derived from the coil regions of known structures
    • Swindells, M. B., MacArthur, M. W., and Thornton, J. M. (1995) Intrinsic phi, psi propensities of amino acids, derived from the coil regions of known structures, Nat. Struct. Biol. 2, 596-603.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 596-603
    • Swindells, M.B.1    MacArthur, M.W.2    Thornton, J.M.3
  • 19
    • 0037610743 scopus 로고    scopus 로고
    • Role of backbone solvation and electrostatics in generating preferred peptide backbone conformations: Distributions of phi
    • Avbelj, F., and Baldwin, R. L. (2003) Role of backbone solvation and electrostatics in generating preferred peptide backbone conformations: distributions of phi, Proc. Natl. Acad. Sci., U.S.A. 100, 5742-5747.
    • (2003) Proc. Natl. Acad. Sci., U.S.A. , vol.100 , pp. 5742-5747
    • Avbelj, F.1    Baldwin, R.L.2
  • 20
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins
    • Chou, P. Y., and Fasman, G. D. (1974) Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins, Biochemistry 13, 211-222.
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 21
    • 0030320442 scopus 로고    scopus 로고
    • The concept of a random coil. Residual structure in peptides and denatured proteins
    • Smith, L. J., Fiebig, K. M., Schwalbe, H., and Dobson, C. M. (1996) The concept of a random coil. Residual structure in peptides and denatured proteins, Fold Des. 1, R95-106.
    • (1996) Fold Des. , vol.1
    • Smith, L.J.1    Fiebig, K.M.2    Schwalbe, H.3    Dobson, C.M.4
  • 22
    • 0029063337 scopus 로고
    • Empirical evaluation of the influence of side chains on the conformational entropy of the polypeptide backbone
    • Stites, W. E., and Pranata, J. (1995) Empirical evaluation of the influence of side chains on the conformational entropy of the polypeptide backbone, Proteins 22, 132-140.
    • (1995) Proteins , vol.22 , pp. 132-140
    • Stites, W.E.1    Pranata, J.2
  • 23
    • 0032769468 scopus 로고    scopus 로고
    • The "random-coil" state of proteins: Comparison of database statistics and molecular simulations
    • O'Connell, T. M., Wang, L., Tropsha, A., and Hermans, J. (1999) The "random-coil" state of proteins: comparison of database statistics and molecular simulations, Proteins 36, 407-418.
    • (1999) Proteins , vol.36 , pp. 407-418
    • O'Connell, T.M.1    Wang, L.2    Tropsha, A.3    Hermans, J.4
  • 25
    • 0028790273 scopus 로고
    • Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation
    • Serrano, L. (1995) Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation, J. Mol. Biol. 254, 322-333.
    • (1995) J. Mol. Biol. , vol.254 , pp. 322-333
    • Serrano, L.1
  • 27
    • 0036400325 scopus 로고    scopus 로고
    • Is polyproline II a major backbone conformation in unfolded proteins?
    • Shi, Z., Woody, R. W., and Kallenbach, N. R. (2002) Is polyproline II a major backbone conformation in unfolded proteins? Adv. Prot. Chem. 62, 163-240.
    • (2002) Adv. Prot. Chem. , vol.62 , pp. 163-240
    • Shi, Z.1    Woody, R.W.2    Kallenbach, N.R.3
  • 28
    • 0038344087 scopus 로고    scopus 로고
    • Stable conformations of tripeptides in aqueous solution studied by UV circular dichroism spectroscopy
    • Eker, F., Griebenow, K., and Schweitzer-Stenner, R. (2003) Stable conformations of tripeptides in aqueous solution studied by UV circular dichroism spectroscopy. J. Am. Chem. Soc. 125, 8178-8185.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8178-8185
    • Eker, F.1    Griebenow, K.2    Schweitzer-Stenner, R.3
  • 29
    • 0036784642 scopus 로고    scopus 로고
    • A simple model for polyproline II structure in unfolded states of alanine-based peptides
    • Pappu, R. V., and Rose, G. D. (2002) A simple model for polyproline II structure in unfolded states of alanine-based peptides, Protein Sci. 10, 2437-2455.
    • (2002) Protein Sci. , vol.10 , pp. 2437-2455
    • Pappu, R.V.1    Rose, G.D.2
  • 30
    • 0036402323 scopus 로고    scopus 로고
    • Determinants of the polyproline II helix from modeling studies
    • Creamer, T. P., and Campbell, M. N. (2002) Determinants of the polyproline II helix from modeling studies, Adv. Protein Chem. 62, 263-282.
    • (2002) Adv. Protein Chem. , vol.62 , pp. 263-282
    • Creamer, T.P.1    Campbell, M.N.2
  • 31
    • 0026355426 scopus 로고
    • Reassessment of the random coil conformation: Vibrational CD study of proline oligopeptides and related polypeptides
    • Dukor, R. K., and Keiderling, T. A. (1991) Reassessment of the random coil conformation: vibrational CD study of proline oligopeptides and related polypeptides, Biopolymers 31, 1747-1761.
    • (1991) Biopolymers , vol.31 , pp. 1747-1761
    • Dukor, R.K.1    Keiderling, T.A.2
  • 32
    • 0029842116 scopus 로고    scopus 로고
    • Residual structure in unfolded proteins revealed by Raman optical activity
    • Wilson, G., Hecht, L., and Barron, L. D. (1996) Residual structure in unfolded proteins revealed by Raman optical activity, Biochemistry 35, 12518-12525.
    • (1996) Biochemistry , vol.35 , pp. 12518-12525
    • Wilson, G.1    Hecht, L.2    Barron, L.D.3
  • 33
    • 0036400324 scopus 로고    scopus 로고
    • Unfolded peptides and proteins studied with infrared absorption and vibrational circular dichroism spectra
    • Keiderling, T. A., and Xu, Q. (2002) Unfolded peptides and proteins studied with infrared absorption and vibrational circular dichroism spectra, Adv. Protein Chem. 62, 111-161.
    • (2002) Adv. Protein Chem. , vol.62 , pp. 111-161
    • Keiderling, T.A.1    Xu, Q.2
  • 34
    • 0036784642 scopus 로고    scopus 로고
    • A simple model for polyproline II structure in unfolded states of alanine-based peptides
    • Pappu, R. V., and Rose, G. D. (2002) A simple model for polyproline II structure in unfolded states of alanine-based peptides, Protein Sci. 11, 2437-2455.
    • (2002) Protein Sci. , vol.11 , pp. 2437-2455
    • Pappu, R.V.1    Rose, G.D.2
  • 35
    • 1542366657 scopus 로고    scopus 로고
    • Role of solvent in determining conformational preferences of alanine dipeptide in water
    • Drozdov, A. N., Grossfield, A., and Pappu, R. V. (2004) Role of solvent in determining conformational preferences of alanine dipeptide in water, J. Am. Chem. Soc. 126, 2574-2581.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2574-2581
    • Drozdov, A.N.1    Grossfield, A.2    Pappu, R.V.3
  • 36
    • 1842500992 scopus 로고    scopus 로고
    • Polyproline II helix is the preferred conformation for unfolded polyalanine in water
    • Mezei, M., Fleming, P. J., Srinivasan, R., and Rose, G. D. (2004) Polyproline II helix is the preferred conformation for unfolded polyalanine in water. Proteins 55, 502-507.
    • (2004) Proteins , vol.55 , pp. 502-507
    • Mezei, M.1    Fleming, P.J.2    Srinivasan, R.3    Rose, G.D.4
  • 37
    • 1842500993 scopus 로고    scopus 로고
    • Unfolded state of polyalanine is a segmented polyproline II helix
    • Kentsis, A., Mezei, M., Gindin, T., and Osman, R. (2004) Unfolded state of polyalanine is a segmented polyproline II helix, Proteins 55, 493-501.
    • (2004) Proteins , vol.55 , pp. 493-501
    • Kentsis, A.1    Mezei, M.2    Gindin, T.3    Osman, R.4
  • 38
    • 0345862082 scopus 로고    scopus 로고
    • Characterization of nonalpha helical conformations in Ala peptides
    • Garcia, A. E. (2004) Characterization of nonalpha helical conformations in Ala peptides, Polymer 45, 669-676.
    • (2004) Polymer , vol.45 , pp. 669-676
    • Garcia, A.E.1
  • 39
    • 2442522724 scopus 로고    scopus 로고
    • Short sequences of nonproline residues can adopt the polyproline II helical conformation
    • Chellgren, B. W., and Creamer, T. P. (2004) Short sequences of nonproline residues can adopt the polyproline II helical conformation, Biochemistry 43, 5864-5869.
    • (2004) Biochemistry , vol.43 , pp. 5864-5869
    • Chellgren, B.W.1    Creamer, T.P.2
  • 42
    • 0027474991 scopus 로고
    • Left-handed polyproline II helices commonly occur in globular proteins
    • Adzhubei, A. A., and Sternberg, M. J. (1993) Left-handed polyproline II helices commonly occur in globular proteins, J. Mol. Biol. 229, 472-493.
    • (1993) J. Mol. Biol. , vol.229 , pp. 472-493
    • Adzhubei, A.A.1    Sternberg, M.J.2
  • 43
    • 1342268081 scopus 로고    scopus 로고
    • Steric restrictions in protein folding: An alpha-helix cannot be followed by a contiguous beta-strand
    • Fitzkee, N. C., and Rose, G. D. (2004) Steric restrictions in protein folding: an alpha-helix cannot be followed by a contiguous beta-strand, Protein Sci. 13, 633-639.
    • (2004) Protein Sci. , vol.13 , pp. 633-639
    • Fitzkee, N.C.1    Rose, G.D.2
  • 44
    • 0043180474 scopus 로고    scopus 로고
    • PISCES: A protein sequence culling server
    • Wang, G., and Dunbrack, R. L., Jr. (2003) PISCES: a protein sequence culling server, Bioinformatics 19, 1589-1591.
    • (2003) Bioinformatics , vol.19 , pp. 1589-1591
    • Wang, G.1    Dunbrack Jr., R.L.2
  • 45
    • 0021755764 scopus 로고
    • Solvent accessible surface area and excluded volume in proteins. Analytical equations for overlapping spheres and implications for the hydrophobic effect
    • Richmond, T. J. (1984) Solvent accessible surface area and excluded volume in proteins. Analytical equations for overlapping spheres and implications for the hydrophobic effect, J. Mol. Biol. 178, 63-89.
    • (1984) J. Mol. Biol. , vol.178 , pp. 63-89
    • Richmond, T.J.1
  • 47
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and 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
  • 48
    • 0028226386 scopus 로고
    • Hydrogen bond strength and beta-sheet propensities: The role of a side chain blocking effect
    • Bai, Y., and Englander, S. W. (1994) Hydrogen bond strength and beta-sheet propensities: the role of a side chain blocking effect, Proteins 18, 262-266.
    • (1994) Proteins , vol.18 , pp. 262-266
    • Bai, Y.1    Englander, S.W.2
  • 49
    • 0031808074 scopus 로고    scopus 로고
    • A helix propensity scale based on experimental studies of peptides and proteins
    • Pace, C. N., and Scholtz, J. M. (1998) A helix propensity scale based on experimental studies of peptides and proteins, Biophys. J. 75, 422-427.
    • (1998) Biophys. J. , vol.75 , pp. 422-427
    • Pace, C.N.1    Scholtz, J.M.2
  • 50
    • 0028175780 scopus 로고
    • A thermodynamic scale for the beta-sheet forming tendencies of the amino acids
    • Smith, C. K., Withka, J. M., and Regan, L. (1994) A thermodynamic scale for the beta-sheet forming tendencies of the amino acids, Biochemistry 33, 5510-5517.
    • (1994) Biochemistry , vol.33 , pp. 5510-5517
    • Smith, C.K.1    Withka, J.M.2    Regan, L.3
  • 51
    • 0028792105 scopus 로고
    • Guidelines for protein design: The energetics of beta sheet side chain interactions
    • Smith, C. K., and Regan, L. (1995) Guidelines for protein design: the energetics of beta sheet side chain interactions, Science 270, 980-982.
    • (1995) Science , vol.270 , pp. 980-982
    • Smith, C.K.1    Regan, L.2
  • 52
    • 0027998757 scopus 로고
    • Context is a major determinant of beta-sheet propensity
    • Minor, D. L., Jr., and Kim, P. S. (1994) Context is a major determinant of beta-sheet propensity, Nature 371, 264-267.
    • (1994) Nature , vol.371 , pp. 264-267
    • Minor Jr., D.L.1    Kim, P.S.2
  • 53
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K. A. (1990) Dominant forces in protein folding. Biochemistry 29, 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 54
    • 0033529861 scopus 로고    scopus 로고
    • Intrinsic beta-sheet propensities result from van der Waals interactions between side chains and the local backbone
    • Street, A. G., and Mayo, S. L. (1999) Intrinsic beta-sheet propensities result from van der Waals interactions between side chains and the local backbone, Proc. Natl. Acad. Sci., U.S.A. 96, 9074-9076.
    • (1999) Proc. Natl. Acad. Sci., U.S.A. , vol.96 , pp. 9074-9076
    • Street, A.G.1    Mayo, S.L.2
  • 55
    • 0029900846 scopus 로고    scopus 로고
    • The magnitude of the backbone conformational entropy change in protein folding
    • D'Aquino, J. A., Gomez, J., Hilser, V. J., Lee, K. H., Amzel, L. M., and Freire, E. (1996) The magnitude of the backbone conformational entropy change in protein folding, Proteins 25, 143-156.
    • (1996) Proteins , vol.25 , pp. 143-156
    • D'Aquino, J.A.1    Gomez, J.2    Hilser, V.J.3    Lee, K.H.4    Amzel, L.M.5    Freire, E.6
  • 56
    • 0028178865 scopus 로고
    • Alpha-helix-forming propensities in peptides and proteins
    • Creamer, T. P., and Rose, G. D. (1994) Alpha-helix-forming propensities in peptides and proteins, Proteins 19, 85-97.
    • (1994) Proteins , vol.19 , pp. 85-97
    • Creamer, T.P.1    Rose, G.D.2
  • 58
    • 7044264212 scopus 로고    scopus 로고
    • Look-up tables for protein solvent accessibility prediction and nearest neighbor effect analysis
    • Wang, J. Y., Ahmad, S., Gromiha, M. M., and Sarai, A. (2004) Look-up tables for protein solvent accessibility prediction and nearest neighbor effect analysis, Biopolymers 75, 209-216.
    • (2004) Biopolymers , vol.75 , pp. 209-216
    • Wang, J.Y.1    Ahmad, S.2    Gromiha, M.M.3    Sarai, A.4
  • 59
    • 0000668407 scopus 로고
    • Theory of the phase transition between helix and random coil in polypeptide chains
    • Zimm, G. H., and 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, G.H.1    Bragg, J.K.2
  • 60
    • 0000333671 scopus 로고
    • On the theory of the helix-coil transition in polypeptides
    • Lifson, S., and Roig, A. (1961) On the theory of the helix-coil transition in polypeptides, J. Chem. Phys. 34, 1963-1974.
    • (1961) J. Chem. Phys. , vol.34 , pp. 1963-1974
    • Lifson, S.1    Roig, A.2
  • 61
    • 84984083490 scopus 로고
    • Statistical mechanics of noncovalent bonds in polyamino acids. 4. Matrix treatment of hydrophobic bonds in random coil and of helix-coil transition for chains of arbitrary length
    • Poland, D. C., and Scheraga, H. A. (1965) Statistical Mechanics of Noncovalent Bonds in Polyamino Acids. 4. Matrix Treatment of Hydrophobic Bonds in Random Coil and of Helix-Coil Transition for Chains of Arbitrary Length, Biopolymers 3, 315.
    • (1965) Biopolymers , vol.3 , pp. 315
    • Poland, D.C.1    Scheraga, H.A.2
  • 62
    • 0016089450 scopus 로고
    • Molecular theory of helix-coil transition in poly(amino acids). 4. Evaluation and analysis of S for poly(L-valine) in absence and presence of water
    • Go, M., Hesselin, F. T., Go, N., and Scheraga, H. A. (1974) Molecular Theory of Helix-Coil Transition in Poly(Amino Acids). 4. Evaluation and Analysis of S for Poly(L-Valine) in Absence and Presence of Water, Macromolecules 7, 459-467.
    • (1974) Macromolecules , vol.7 , pp. 459-467
    • Go, M.1    Hesselin, F.T.2    Go, N.3    Scheraga, H.A.4
  • 63
    • 0032972986 scopus 로고    scopus 로고
    • Is protein folding hierarchic? I. Local structure and peptide folding
    • Baldwin, R. L., and Rose, G. D. (1999) Is protein folding hierarchic? I. Local structure and peptide folding. Trends Biochem Sci 24, 26-33.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 26-33
    • Baldwin, R.L.1    Rose, G.D.2


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