메뉴 건너뛰기




Volumn 61, Issue 4, 2003, Pages 189-201

Dipole interaction model predicted π-π* circular dichroism of cyclo(L-Pro)3 using structures created by semi-empirical, ab initio, and molecular mechanics methods

Author keywords

cis trans peptide bonds; Dipole interaction model; Molecular modeling; UV circular dichroism

Indexed keywords

CYCLOPEPTIDE; PROLINE; SYNTHETIC PEPTIDE;

EID: 0037381708     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3011.2003.00046.x     Document Type: Article
Times cited : (14)

References (33)
  • 1
    • 0016997976 scopus 로고
    • Structure and conformation of cyclo(tri-L-prolyl) in the crystalline state
    • Druyan, M.E., Coulter, C.L., Walter, R., Kartha, G. & Ambady, G.K. (1976) Structure and conformation of cyclo(tri-L-prolyl) in the crystalline state. J. Am. Chem. Soc. 98, 5496-5502.
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 5496-5502
    • Druyan, M.E.1    Coulter, C.L.2    Walter, R.3    Kartha, G.4    Ambady, G.K.5
  • 2
    • 0015117073 scopus 로고
    • Cyclic peptides. I. Cyclo(tri-L-prolyl) and derivatives. Synthesis and molecular conformation from nuclear magnetic resonance
    • Deber, C.M., Torchia, D.A. & Blout, E.R. (1971) Cyclic peptides. I. Cyclo(tri-L-prolyl) and derivatives. Synthesis and molecular conformation from nuclear magnetic resonance. J. Am. Chem. Soc. 93, 4893-4897.
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 4893-4897
    • Deber, C.M.1    Torchia, D.A.2    Blout, E.R.3
  • 3
    • 0016390628 scopus 로고
    • 1H nuclear magnetic resonance evidence for slow cis-trans rotations in a cyclic tetrapeptide
    • 1H nuclear magnetic resonance evidence for slow cis-trans rotations in a cyclic tetrapeptide. J. Am. Chem. Soc. 96, 4015-4017.
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 4015-4017
    • Deber, C.M.1    Fossel, E.T.2    Blout, E.R.3
  • 4
    • 85004829976 scopus 로고
    • Stereochemical studies of cyclic peptides XIV. Conformational analysis of cyclic tripeptides
    • Ramakrishnan, C., Ramnarayan, K. & Manjula, G. (1987) Stereochemical studies of cyclic peptides XIV. Conformational analysis of cyclic tripeptides. J. Pept. Protein Res 29, 657-671.
    • (1987) J. Pept. Protein Res. , vol.29 , pp. 657-671
    • Ramakrishnan, C.1    Ramnarayan, K.2    Manjula, G.3
  • 6
    • 0001529568 scopus 로고    scopus 로고
    • Theoretical and experimental circular cichroic spectra of the novel helical foldamer poly[(1R,2R]-trans-2aminocyclopentanecarboxylic acid]
    • Applequist, J.A., Bode, K.A., Appella, D.H., Christianson, L.A. & Gellman, S.H. (1998) Theoretical and experimental circular cichroic spectra of the novel helical foldamer poly[(1R,2R]-trans-2aminocyclopentanecarboxylic acid]. J. Am. Chem. Soc. 120, 4891-4892.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 4891-4892
    • Applequist, J.A.1    Bode, K.A.2    Appella, D.H.3    Christianson, L.A.4    Gellman, S.H.5
  • 7
    • 0001911969 scopus 로고    scopus 로고
    • Circular dichroism of peptides and proteins
    • Berova, N., Nakanishi, K. & Woody, R.W., eds. John Wiley & Sons, New York
    • Sreerama, N. & Woody, R.W. (2000) Circular dichroism of peptides and proteins. In: Circular Dichroism Principles and Applications (Berova, N., Nakanishi, K. & Woody, R.W., eds), pp. 601-620. John Wiley & Sons, New York.
    • (2000) Circular Dichroism Principles and Applications , pp. 601-620
    • Sreerama, N.1    Woody, R.W.2
  • 8
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy
    • Sreerama, N., Venyaminov, S.Y., Yu, S. & Woody, R.W. (1999) Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy. Protein Sci. 8, 370-380.
    • (1999) Protein Sci. , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.Y.2    Yu, S.3    Woody, R.W.4
  • 9
    • 0002215428 scopus 로고    scopus 로고
    • Determination of protein secondary structure in circular dichrosim and the conformational analysis of biomolecules
    • Fasman, G.D., ed. Plenum Press, New York
    • Venyaminov, S.Y. & Yang, J.T. (1996) Determination of protein secondary structure in circular dichrosim and the conformational analysis of biomolecules. In: Circular Dichroism and the Conformational Analysis of Biomolecules (Fasman, G.D., ed.), pp. 69-107. Plenum Press, New York
    • (1996) Circular Dichroism and the Conformational Analysis of Biomolecules , pp. 69-107
    • Venyaminov, S.Y.1    Yang, J.T.2
  • 10
    • 84985720134 scopus 로고
    • Theoretical π-π* absorption and circular dichroic spectra of helical poly(L-proline) forms I and II
    • Applequist, J.A. (1981) Theoretical π-π* absorption and circular dichroic spectra of helical poly(L-proline) forms I and II. Biopolymers 20, 2311-2322.
    • (1981) Biopolymers , vol.20 , pp. 2311-2322
    • Applequist, J.A.1
  • 11
    • 0021189670 scopus 로고
    • Theoretical π-π* absorption, circular dichroic, and linear dichroic spectra of collagen triple helices
    • Caldwell, J.W. & Applequist, J.A. (1984) Theoretical π-π* absorption, circular dichroic, and linear dichroic spectra of collagen triple helices. Biopolymers 23, 1891-1904.
    • (1984) Biopolymers , vol.23 , pp. 1891-1904
    • Caldwell, J.W.1    Applequist, J.A.2
  • 12
    • 0029813759 scopus 로고    scopus 로고
    • Force field dependence of Boltzmann weighting factors on predicted π-π* circular dichroic spectra of cyclo(Gly-Pro-Gly)2
    • MacFarlane, K.J., Humbert, M.M. & Thomasson, K.A. (1996) Force field dependence of Boltzmann weighting factors on predicted π-π* circular dichroic spectra of cyclo(Gly-Pro-Gly)2. Int. J. Pept. Protein Res. 47, 447-459.
    • (1996) Int. J. Pept. Protein Res. , vol.47 , pp. 447-459
    • MacFarlane, K.J.1    Humbert, M.M.2    Thomasson, K.A.3
  • 13
    • 0022160202 scopus 로고
    • Theoretical π-π* absorption and circular dichroic spectra of cyclic dipeptides
    • Sathyanarayana, B.K. & Applequist, J.A. (1985) Theoretical π-π* absorption and circular dichroic spectra of cyclic dipeptides. Int. J. Pept. Protein Res. 26, 518-527.
    • (1985) Int. J. Pept. Protein Res. , vol.26 , pp. 518-527
    • Sathyanarayana, B.K.1    Applequist, J.A.2
  • 14
    • 0026143163 scopus 로고
    • Effect of proline ring conformation on theoretical π-π* absorption and CD spectra of helical poly(L-proline] forms I and II
    • Thomasson, K.A. & Applequist, J.A. (1991) Effect of proline ring conformation on theoretical π-π* absorption and CD spectra of helical poly(L-proline] forms I and II. Biopolymers 31, 529-535.
    • (1991) Biopolymers , vol.31 , pp. 529-535
    • Thomasson, K.A.1    Applequist, J.A.2
  • 15
    • 33947091822 scopus 로고
    • An atom dipole interaction model for molecular polarizability. Application to polyatomic molecules and determination of atom polarizabilities
    • Applequist, J.A., Carl, J.R. & Fung, K.-K. (1972) An atom dipole interaction model for molecular polarizability. Application to polyatomic molecules and determination of atom polarizabilities. J. Am. Chem. Soc. 94, 2952-2960.
    • (1972) J. Am. Chem. Soc. , vol.94 , pp. 2952-2960
    • Applequist, J.A.1    Carl, J.R.2    Fung, K.-K.3
  • 16
    • 33645430596 scopus 로고    scopus 로고
    • A new optimization of atom polarizabilities in halomethanes, aldehydes, ketones and amides by way of the atom dipole interaction model
    • Bode, K.A. & Applequist, J.A. (1996) A New optimization of atom polarizabilities in halomethanes, aldehydes, ketones and amides by way of the atom dipole interaction model. J Phys. Chem. 100, 17820-17824.
    • (1996) J Phys. Chem. , vol.100 , pp. 17820-17824
    • Bode, K.A.1    Applequist, J.A.2
  • 17
    • 0001035579 scopus 로고    scopus 로고
    • Improved theoretical π-π* absorption and circular dichroic spectra of helical polypeptides using new polarizabilities of atoms and NC'O chromophores
    • Erratum: (1997) J. Phys. Chem. 101, 9560
    • Bode, K.A. & Applequist, J.A. (1996) Improved theoretical π-π* absorption and circular dichroic spectra of helical polypeptides using new polarizabilities of atoms and NC'O chromophores. J. Phys. Chem. 100, 17825-17834 Erratum: (1997) J. Phys. Chem. 101, 9560.
    • (1996) J. Phys. Chem. , vol.100 , pp. 17825-17834
    • Bode, K.A.1    Applequist, J.A.2
  • 19
    • 0022584627 scopus 로고
    • Theoretical ππ* absorption and circular dichroic spectra of beta-turn model peptides
    • Sathyanarayana, B.K. & Applequist, J.A. (1986) Theoretical ππ* absorption and circular dichroic spectra of beta-turn model peptides. Int. J. Pept. Protein Res. 27, 86-94.
    • (1986) Int. J. Pept. Protein Res. , vol.27 , pp. 86-94
    • Sathyanarayana, B.K.1    Applequist, J.A.2
  • 20
    • 0031539136 scopus 로고    scopus 로고
    • Helix bundles and coiled coils in alpha-spectrin and tropomyosin: A theoretical CD study
    • Bode, K.A. & Applequist, J.A. (1997) Helix bundles and coiled coils in alpha-spectrin and tropomyosin: a theoretical CD study. Biopolymers 42, 855-860.
    • (1997) Biopolymers , vol.42 , pp. 855-860
    • Bode, K.A.1    Applequist, J.A.2
  • 21
    • 0032576160 scopus 로고    scopus 로고
    • Globular protein ultraviolet circular dichroic spectra. Calculation from crystal structures via the dipole interaction model
    • Erratum J. Am Chem. Soc. 120, 13545
    • Bode, K.A. & Applequist, J.A. (1998) Globular protein ultraviolet circular dichroic spectra. Calculation from crystal structures via the dipole interaction model. J. Am. Chem. Soc. 120, 10938-10946 Erratum J. Am Chem. Soc. 120, 13545.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 10938-10946
    • Bode, K.A.1    Applequist, J.A.2
  • 24
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. III. The role of exact exchange
    • Becke, A.D. (1993) Density-functional thermochemistry. III. The role of exact exchange. J. Chem. Phys. 98, 5648-5652.
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 25
    • 11744256643 scopus 로고
    • Molecular interactions in solution: An overview of methods based on continuous distributions of the solvent
    • Tomasi, J. & Persico, M. (1994) Molecular interactions in solution: an overview of methods based on continuous distributions of the solvent. Chem. Rev. 94, 2027-2094.
    • (1994) Chem. Rev. , vol.94 , pp. 2027-2094
    • Tomasi, J.1    Persico, M.2
  • 26
    • 84962440518 scopus 로고    scopus 로고
    • Analytical derivatives for geometry optimization in solvation continuum models. II. Numerical applications
    • Cances, E., Mennucci, B. & Tomasi, J. (1998) Analytical derivatives for geometry optimization in solvation continuum models. II. Numerical applications. J. Chem. Phys. 109, 260-266.
    • (1998) J. Chem. Phys. , vol.109 , pp. 260-266
    • Cances, E.1    Mennucci, B.2    Tomasi, J.3
  • 28
    • 0001242416 scopus 로고
    • A full polarizability treatment of the π-π* absorption and circular dichroic spectra of alpha-helical polypeptides
    • Erratum: (1980) J. Chem. Phys. 73(7), 3521
    • Applequist, J.A. (1979) A full polarizability treatment of the π-π* absorption and circular dichroic spectra of alpha-helical polypeptides. J. Chem. Phys. 71, 4332-4338 Erratum: (1980) J. Chem. Phys. 73(7), 3521.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4332-4338
    • Applequist, J.A.1
  • 29
    • 0001552515 scopus 로고
    • Conformational analysis of proline rings from proton spin-spin coupling constants and force-field calculations: Application to three cyclic tripeptides
    • -deLeeuw, F.A.A.M., Altona, C., Kessler, H., Bermel, W., Friedrich, A., Krack, G. & Hull, W. (1983) Conformational analysis of proline rings from proton spin-spin coupling constants and force-field calculations: application to three cyclic tripeptides. J. Am. Chem. Soc. 105, 2237-2246.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 2237-2246
    • DeLeeuw, F.A.A.M.1    Altona, C.2    Kessler, H.3    Bermel, W.4    Friedrich, A.5    Krack, G.6    Hull, W.7
  • 30
    • 0000915841 scopus 로고
    • Description of steric relationships across single bonds
    • Klyne, W. & Prelog, V. (1960) Description of steric relationships across single bonds. Experientia 16, 521-523.
    • (1960) Experientia , vol.16 , pp. 521-523
    • Klyne, W.1    Prelog, V.2
  • 31
    • 0025002213 scopus 로고
    • Bond-optimized ring closure for proline: Comparison of conformations and semiempirical energies with small molecule X-ray structures
    • Thomasson, K.A. & Applequist, J.A. (1990) Bond-optimized ring closure for proline: comparison of conformations and semiempirical energies with small molecule X-ray structures. Biopolymers 30, 437-450.
    • (1990) Biopolymers , vol.30 , pp. 437-450
    • Thomasson, K.A.1    Applequist, J.A.2
  • 33
    • 0014402284 scopus 로고
    • Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units
    • Venkatachalam, C.M. (1968) Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units. Biochim. Biophys. Acta 168, 397-401.
    • (1968) Biochim. Biophys. Acta , vol.168 , pp. 397-401
    • Venkatachalam, C.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.