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Volumn 248, Issue 2, 1995, Pages 374-384

Coulombic attractions between partially chargedmain-chain atoms stabilise the right-handed twist found in most β-strands

Author keywords

Electrostatic; Polyproline; Ramachandran plot; Twist; sheet

Indexed keywords

AMINO ACID; CARBON; COLLAGEN; OXYGEN; POLYPEPTIDE; PROLINE;

EID: 0029078444     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(95)80057-3     Document Type: Article
Times cited : (98)

References (43)
  • 1
    • 0027474991 scopus 로고
    • Left-handed polyproline II helices commonly occur in globular proteins
    • Adzhubei, A. A. & Sternberg, M. J. E. (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.E.2
  • 4
    • 0001208994 scopus 로고
    • The crystal structure of alloxan
    • Bolton, W. (1964). The crystal structure of alloxan. Acta Crystallogr. 17, 147-152.
    • (1964) Acta Crystallogr , vol.17 , pp. 147-152
    • Bolton, W.1
  • 5
    • 0002962709 scopus 로고
    • The crystal structure of triketoindane (Anhydrous ninhyrin). A structure showing close C=0 or c=N interactions
    • Bolton, W. (1965). The crystal structure of triketoindane (anhydrous ninhyrin). A structure showing close C=0 or c=N interactions. Acta Crystallogr. 18, 5-10.
    • (1965) Acta Crystallogr , vol.18 , pp. 5-10
    • Bolton, W.1
  • 6
    • 84986512474 scopus 로고    scopus 로고
    • States, D.)., Swaminathan, S. & Karplus, M. (1983). CHARMM: A program for macromolecular energy minimisation and dynamics calculations
    • Brooks, B. R., Bruccoleri, R. E., Olafson, B. D., States, D.)., Swaminathan, S. & Karplus, M. (1983). CHARMM: a program for macromolecular energy minimisation and dynamics calculations. J. Comput. Chem. 4, 187-217.
    • J. Comput. Chem. , vol.4 , pp. 187-217
    • Brooks, B.R.1    Bruccoleri, R.E.2    Olafson, B.D.3
  • 7
    • 0041140017 scopus 로고
    • Simulations of peptide conformational dynamics and thermodynamics
    • Brooks, C. L., III & Case, D. A. (1993). Simulations of peptide conformational dynamics and thermodynamics. Chem. Rev. 93, 2487-2502.
    • (1993) Chem. Rev. , vol.93 , pp. 2487-2502
    • Brooks, C.L.1    Case, D.A.2
  • 8
    • 0004166732 scopus 로고
    • Structure correlation: The chemical point of view
    • Burgi, H. D. & Dunitz, J. D., VCH, Weinheim & New York
    • Burghi, H. B. & Dunitz, J. D. (1994). Structure correlation: the chemical point of view. In Structure Correlation (Burgi, H. D. & Dunitz, J. D., eds), pp. 163-204, VCH, Weinheim & New York.
    • (1994) Structure Correlation , pp. 163-204
    • Burghi, H.B.1    Dunitz, J.D.2
  • 9
    • 0001135446 scopus 로고
    • Chemical reaction paths. IV. Aspects of O … C=0 interactions in crystals
    • Burgi, H. B., Dunitz, J. D. & Shefter, E. (1974). Chemical reaction paths. IV. Aspects of O … C=0 interactions in crystals. Acta Crystallogr. sect. B, 30, 1517-1527.
    • (1974) Acta Crystallogr. Sect. B , vol.30 , pp. 1517-1527
    • Burgi, H.B.1    Dunitz, J.D.2    Shefter, E.3
  • 10
    • 0015914783 scopus 로고
    • Conformations of (3-pleated sheets in proteins
    • Chothia, C. (1973). Conformations of (3-pleated sheets in proteins. J Mol. Biol. 75, 295-302.
    • (1973) J Mol. Biol. , vol.75 , pp. 295-302
    • Chothia, C.1
  • 11
    • 0021095115 scopus 로고
    • Coiling of P-pleated sheets
    • Chothia, C. (1983). Coiling of P-pleated sheets. J. Mol. Biol. 163, 107-117.
    • (1983) J. Mol. Biol. , vol.163 , pp. 107-117
    • Chothia, C.1
  • 12
    • 0001244377 scopus 로고
    • The origin of the right-handed twist of P-sheets of poly(L-valine) chains
    • Chou, K.-C. & Scheraga, H. A. (1982). The origin of the right-handed twist of P-sheets of poly(l-valine) chains. Proc. Nat. Acad. Sci., U.S.A. 79, 7047-7051.
    • (1982) Proc. Nat. Acad. Sci., U.S.A. , vol.79 , pp. 7047-7051
    • Chou, K.-C.1    Scheraga, H.A.2
  • 13
    • 0020491376 scopus 로고
    • Structure of P-sheets. Origin of the right-handed twist and of the increased stability of antiparallel over parallel sheets
    • Chou, K.-C., Pottle, M., Nemethy, G., Ueda, Y. & Scheraga, H. A. (1982). Structure of P-sheets. Origin of the right-handed twist and of the increased stability of antiparallel over parallel sheets. J Mol. Biol. 162, 89-112.
    • (1982) J Mol. Biol. , vol.162 , pp. 89-112
    • Chou, K.-C.1    Pottle, M.2    Nemethy, G.3    Ueda, Y.4    Scheraga, H.A.5
  • 14
    • 0001311307 scopus 로고
    • The effect of amino acid composition on the twist and relative stability of parallel and antiparallel P-sheets
    • Chou, K.-C., Nemethy, G. & Scheraga, H. A. (1983a). The effect of amino acid composition on the twist and relative stability of parallel and antiparallel P-sheets. Biochemistry, 22, 6213-6221.
    • (1983) Biochemistry , vol.22 , pp. 6213-6221
    • Chou, K.-C.1    Nemethy, G.2    Scheraga, H.A.3
  • 15
    • 0021095536 scopus 로고
    • The role of inter-chain interaction in the stabilisation of the right-handed twist of P-sheets
    • Chou, K.-C., Nemethy, G. & Scheraga, H. A. (1983b). The role of inter-chain interaction in the stabilisation of the right-handed twist of P-sheets. J Mol. Biol. 168, 389-407.
    • (1983) J Mol. Biol. , vol.168 , pp. 389-407
    • Chou, K.-C.1    Nemethy, G.2    Scheraga, H.A.3
  • 16
    • 0343862138 scopus 로고
    • Energetics of interactions of regular structural elements in proteins
    • Chou, K.-C., Nemethy, G. & Scheraga, H. A. (1990). Energetics of interactions of regular structural elements in proteins. Acc. Chem. Res. 23, 134-141.
    • (1990) Acc. Chem. Res. , vol.23 , pp. 134-141
    • Chou, K.-C.1    Nemethy, G.2    Scheraga, H.A.3
  • 18
    • 0001626451 scopus 로고
    • Packing analysis of organic crystals containing C=0 or C=N groups. J
    • Gavezzotti, A. (1990). Packing analysis of organic crystals containing C=0 or C=N groups. J Phys. Chem. 94, 4319-4325.
    • (1990) Phys. Chem. , vol.94 , pp. 4319-4325
    • Gavezzotti, A.1
  • 19
    • 0016399126 scopus 로고
    • Energy functions for peptides and proteins. II. The amide hydrogen bond and calculation of amide crystal properties
    • Hagler, A. T. & Lifson, S. (1974). Energy functions for peptides and proteins. II. The amide hydrogen bond and calculation of amide crystal properties. J. Amer. Chem. Soc. 96, 5327-5335.
    • (1974) J. Amer. Chem. Soc. , vol.96 , pp. 5327-5335
    • Hagler, A.T.1    Lifson, S.2
  • 20
    • 6344256147 scopus 로고
    • CFF studies of intermolecular forces in hydrogen-bonded crystals 2. A Benchmark for the objective comparison of alternative force fields
    • Hagler, A. T., Lifson, S. & Dauber, P. (1979). CFF studies of intermolecular forces in hydrogen-bonded crystals 2. A Benchmark for the objective comparison of alternative force fields. J Amer. Chem. Soc. 101, 5122-5130.
    • (1979) J Amer. Chem. Soc. , vol.101 , pp. 5122-5130
    • Hagler, A.T.1    Lifson, S.2    Dauber, P.3
  • 21
    • 33645941402 scopus 로고
    • The OPLS potential functions for proteins. Energy minimization for crystals of cyclic peptides and crambin
    • Jorgenson, W. L. & Tirado-Rives, J. (1988). The OPLS potential functions for proteins. Energy minimization for crystals of cyclic peptides and crambin. J. Amer. Chem. Soc. 110, 1657-1666.
    • (1988) J. Amer. Chem. Soc. , vol.110 , pp. 1657-1666
    • Jorgenson, W.L.1    Tirado-Rives, J.2
  • 22
    • 0025048105 scopus 로고
    • Molecular dynamics simulations in biology
    • Karplus, M. & Petsko, G. A. (1990). Molecular dynamics simulations in biology Nature (London), 347, 631-639.
    • (1990) Nature (London) , vol.347 , pp. 631-639
    • Karplus, M.1    Petsko, G.A.2
  • 23
    • 6344256147 scopus 로고
    • Consistent force field studies of intermolecular forces in hydrogen bonded crystals
    • Lifson, S., Hagler, A. T. & Dauber, P. (1979). Consistent force field studies of intermolecular forces in hydrogen bonded crystals. J Amer. Chem. Soc. 101, 5111-5121.
    • (1979) J Amer. Chem. Soc. , vol.101 , pp. 5111-5121
    • Lifson, S.1    Hagler, A.T.2    Dauber, P.3
  • 24
    • 0029048210 scopus 로고
    • Coulombic interactions between partially charged main-chain atoms not hydrogen-bonded to each other influence the conformations of a-helices and antiparallel P-sheet. A new method for analysing forces between hydrogen bonding groups in proteins includes all the Coulombic interactions
    • Maccallum, P. H., Poet, R. & Milner-White, E. J. (1995). Coulombic interactions between partially charged main-chain atoms not hydrogen-bonded to each other influence the conformations of a-helices and antiparallel P-sheet. A new method for analysing forces between hydrogen bonding groups in proteins includes all the Coulombic interactions. J. Mol. Biol. 248, 361-373.
    • (1995) J. Mol. Biol. , vol.248 , pp. 361-373
    • Maccallum, P.H.1    Poet, R.2    Milner-White, E.J.3
  • 25
    • 0025690309 scopus 로고
    • Situations of gamma-turns in proteins; their relationship to a-helices, P-sheets and ligand binding sites
    • Milner-White, E. J. (1990). Situations of gamma-turns in proteins; their relationship to a-helices, P-sheets and ligand binding sites. J. Mol. Biol. 216, 385-397.
    • (1990) J. Mol. Biol. , vol.216 , pp. 385-397
    • Milner-White, E.J.1
  • 26
    • 0000302360 scopus 로고
    • Loops, bulges, turns and hairpins in proteins
    • Milner-White, E. J. & Poet, R. (1987). Loops, bulges, turns and hairpins in proteins. Trends Biochem. Sci. 12, 189-193.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 189-193
    • Milner-White, E.J.1    Poet, R.2
  • 27
    • 0027080914 scopus 로고
    • Pyrrolidine ring puckering in proteins and polypeptides
    • Milner-White, E. J., Bell, L. H. & Maccallum, P. H. (1992). Pyrrolidine ring puckering in proteins and polypeptides. J Mol. Biol. 228, 725-734.
    • (1992) J Mol. Biol. , vol.228 , pp. 725-734
    • Milner-White, E.J.1    Bell, L.H.2    Maccallum, P.H.3
  • 28
    • 0345296859 scopus 로고
    • Potential Energy Functions
    • Goodfellow, J. M. & Moss, D. S., Ellis Horwood, Chichester, UK
    • Price, S. L. & Goodfellow, J. M. (1992). Potential Energy Functions. In Computer Modelling of Biological Processes (Goodfellow, J. M. & Moss, D. S., eds), pp. 85-100, Ellis Horwood, Chichester, UK.
    • (1992) Computer Modelling of Biological Processes , pp. 85-100
    • Price, S.L.1    Goodfellow, J.M.2
  • 31
    • 0019443447 scopus 로고
    • Protein Anatomy
    • Richardson R. (1981). Protein Anatomy. Adv. Prot. Chem, 34, 167-339.
    • (1981) Adv. Prot. Chem , vol.34 , pp. 167-339
    • Richardson, R.1
  • 33
    • 0020991935 scopus 로고
    • Structural properties of protein P-sheets
    • Salemme, F. R. (1983). Structural properties of protein P-sheets. Prog. Biophys. Mol. Biol. 42, 95-133.
    • (1983) Prog. Biophys. Mol. Biol. , vol.42 , pp. 95-133
    • Salemme, F.R.1
  • 34
    • 0001567029 scopus 로고
    • Structure of polyproline. II
    • Sasiekharan, V. (1959). Structure of polyproline. II. Acta Crystallogr. 12, 897-903.
    • (1959) Acta Crystallogr , vol.12 , pp. 897-903
    • Sasiekharan, V.1
  • 35
    • 0027052447 scopus 로고
    • Inclusion of solation free energy with molecular mechanics energy: Alanyl dipeptide as a test case
    • Schiffer, C. A., Caldwell, J. W., Stroud, R. M. & Kollman, P. A. (1992). Inclusion of solation free energy with molecular mechanics energy: alanyl dipeptide as a test case. Protein Sci. 1, 396-400.
    • (1992) Protein Sci , vol.1 , pp. 396-400
    • Schiffer, C.A.1    Caldwell, J.W.2    Stroud, R.M.3    Kollman, P.A.4
  • 36
    • 0017152045 scopus 로고
    • Extended helical conformation newly observed in protein folding
    • Srinivasan R., Balasubramanian, R. & Rajan, S. S. (1976). Extended helical conformation newly observed in protein folding. Science, 194, 720-722.
    • (1976) Science , vol.194 , pp. 720-722
    • Srinivasan, R.1    Balasubramanian, R.2    Rajan, S.S.3
  • 37
    • 0020807255 scopus 로고
    • Computer simulation of the conformational properties of retro-inverso peptides I
    • Stem, P. S., Chorev, M., Goodman, M. & Hagler, A. T. (1983). Computer simulation of the conformational properties of retro-inverso peptides I. Biopolymers, 22, 1885-1900.
    • (1983) Biopolymers , vol.22 , pp. 1885-1900
    • Stem, P.S.1    Chorev, M.2    Goodman, M.3    Hagler, A.T.4
  • 38
    • 0017073680 scopus 로고
    • On the conformation of proteins: The handedness of the P-strand-a-helix-p-strand unit
    • Sternberg, M. J. E. & Thornton, J. M. (1976). On the conformation of proteins: the handedness of the P-strand-a-helix-p-strand unit. J Mol. Biol. 105, 367-382.
    • (1976) J Mol. Biol. , vol.105 , pp. 367-382
    • Sternberg, M.J.E.1    Thornton, J.M.2
  • 39
    • 0001868266 scopus 로고
    • The fully extended polypeptide conformation
    • Balaram P. & Ramaseshan, S. Eds). Indian Academy of Sciences, Bangalore
    • Toniolo, C. & Benedetti, E. (1991). The fully extended polypeptide conformation. In Molecular Conformation and Biological Interactions (Balaram P. & Ramaseshan, S. Eds). Indian Academy of Sciences, Bangalore.
    • (1991) Molecular Conformation and Biological Interactions
    • Toniolo, C.1    Benedetti, E.2
  • 40
    • 0027386832 scopus 로고
    • Role of tight packing of hydrophobic groups in p-structure
    • Vtyurin, N. (1993). Role of tight packing of hydrophobic groups in p-structure. Proteins: Struct. Fund. Genet. 15, 62-70.
    • (1993) Proteins: Struct. Fund. Genet. , vol.15 , pp. 62-70
    • Vtyurin, N.1
  • 42
    • 0028097921 scopus 로고
    • The structure and function of proline-rich regions in proteins
    • Williamson, M. P. (1994). The structure and function of proline-rich regions in proteins. Biochem. J 297, 249-260.
    • (1994) Biochem. J , vol.297 , pp. 249-260
    • Williamson, M.P.1
  • 43
    • 0017435119 scopus 로고
    • Conformational analysis of the 20 naturally occurring amino acid residues using ECEPP
    • Zimmerman, S. S., Pottle, M. S., Nemethy, G. & Scheraga, H. A. (1977). Conformational analysis of the 20 naturally occurring amino acid residues using ECEPP. Macromolecules, 101, 1-10.
    • (1977) Macromolecules , vol.101 , pp. 1-10
    • Zimmerman, S.S.1    Pottle, M.S.2    Nemethy, G.3    Scheraga, H.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.