메뉴 건너뛰기




Volumn 16, Issue 3, 2010, Pages 126-135

Conformational properties of the residues connected by ester and methylated amide bonds: Theoretical and solid state conformational studies

Author keywords

Conformational analysis; Depsipeptide; DFT calculations; Methylation; X ray structure

Indexed keywords

AMIDE; CHLOROFORM; DEPSIPEPTIDE; ESTER; SOLVENT; WATER;

EID: 76749145508     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1208     Document Type: Article
Times cited : (10)

References (51)
  • 1
    • 76749136975 scopus 로고    scopus 로고
    • Methods of organic chemistry (Houben-Weyl) Tom E22c
    • eds, Georg Thieme Verlag: Stuttgart;
    • Ivanov VT, Mikhaleva II, Methods of organic chemistry (Houben-Weyl) Tom E22c. In: Goodman M, Felix A, Toniolo C (eds). Synthesis of Peptides and Peptidomimetics. Georg Thieme Verlag: Stuttgart; 2003; p 272.
    • (2003) Synthesis of Peptides and Peptidomimetics , pp. 272
    • Ivanov, V.T.1    Mikhaleva II2
  • 2
    • 76749152731 scopus 로고    scopus 로고
    • URL: http://www.chem.qmul.ac.uk/iupac/AminoAcid (3AA-19.6. Depsipeptides).
    • URL: http://www.chem.qmul.ac.uk/iupac/AminoAcid (3AA-19.6. Depsipeptides).
  • 3
    • 0036229133 scopus 로고    scopus 로고
    • Recent developments in depsipeptide research
    • Ballard CE, Yu H, Wang B. Recent developments in depsipeptide research. Curr. Med. Chem. 2002; 9: 471-498.
    • (2002) Curr. Med. Chem , vol.9 , pp. 471-498
    • Ballard, C.E.1    Yu, H.2    Wang, B.3
  • 4
    • 2342633291 scopus 로고    scopus 로고
    • Chemistry and biology of cyclic depsipeptides of medicinal and biological interest
    • Sarabia F, Chammaa S, Ruiz AS, Ortiz LM, Herrera FJL. Chemistry and biology of cyclic depsipeptides of medicinal and biological interest. Curr. Med. Chem. 2004; 11: 1309-1332.
    • (2004) Curr. Med. Chem , vol.11 , pp. 1309-1332
    • Sarabia, F.1    Chammaa, S.2    Ruiz, A.S.3    Ortiz, L.M.4    Herrera, F.J.L.5
  • 5
    • 0344431240 scopus 로고    scopus 로고
    • FR901228, a potent antitumor antibiotic, is a novel histone deacetylase inhibitor
    • Nakajima H, Kim YB, Terano H, Yoshida M, Horinouchi S. FR901228, a potent antitumor antibiotic, is a novel histone deacetylase inhibitor. Exp. Cell Res. 1998; 241: 126-133.
    • (1998) Exp. Cell Res , vol.241 , pp. 126-133
    • Nakajima, H.1    Kim, Y.B.2    Terano, H.3    Yoshida, M.4    Horinouchi, S.5
  • 7
    • 55449094954 scopus 로고    scopus 로고
    • Bishara A, Rudi A, Aknin M, Neumann D, Ben-Califa N, Kashman Y. Taumycins A and B, two bioactive lipodepsipeptides from the madagascar sponge Fascaplysinopsis sp. Org. Lett. 2008; 10: 4307-4309.
    • Bishara A, Rudi A, Aknin M, Neumann D, Ben-Califa N, Kashman Y. Taumycins A and B, two bioactive lipodepsipeptides from the madagascar sponge Fascaplysinopsis sp. Org. Lett. 2008; 10: 4307-4309.
  • 8
    • 56049115106 scopus 로고    scopus 로고
    • 3, a new member of the myxochromide family of secondary metabolites
    • 3, a new member of the myxochromide family of secondary metabolites. J. Nat. Prod. 2008; 71: 1708-1713.
    • (2008) J. Nat. Prod , vol.71 , pp. 1708-1713
    • Ohlendorf, B.1    Kehraus, S.2    König, G.M.3
  • 9
    • 33750374250 scopus 로고    scopus 로고
    • Oh D-C, Jensen PR, FenicalW. Zygosporamide, a cytotoxic cyclic depsipeptide from themarine-derived fungus Zygosporium masonii. Tetrahedron Lett. 2006; 47: 8625-8628.
    • Oh D-C, Jensen PR, FenicalW. Zygosporamide, a cytotoxic cyclic depsipeptide from themarine-derived fungus Zygosporium masonii. Tetrahedron Lett. 2006; 47: 8625-8628.
  • 10
    • 0033538036 scopus 로고    scopus 로고
    • Sansalvamide: A new cytotoxic cyclic depsipeptide produced by a marine fungus of the genus Fusarium
    • Belofsky GN, Jensen PR, FenicalW. Sansalvamide: a new cytotoxic cyclic depsipeptide produced by a marine fungus of the genus Fusarium. Tetrahedron Lett. 1999; 40: 2913-2916.
    • (1999) Tetrahedron Lett , vol.40 , pp. 2913-2916
    • Belofsky, G.N.1    Jensen, P.R.2    FenicalW3
  • 11
    • 0344241060 scopus 로고    scopus 로고
    • A general methodology for automated solid-phase synthesis of depsides and depsipeptides. Preparation of a valinomycin analogue
    • Kuisle O, Quio E, Riguera R. A general methodology for automated solid-phase synthesis of depsides and depsipeptides. Preparation of a valinomycin analogue. J. Org. Chem. 1999; 64: 8063-8075.
    • (1999) J. Org. Chem , vol.64 , pp. 8063-8075
    • Kuisle, O.1    Quio, E.2    Riguera, R.3
  • 12
    • 37049078609 scopus 로고
    • Structure of cereulide, a cyclic dodecadepsipeptide toxin from Bacillus cereus and studies on NMR characteristics of its alkali metal complexes including a conformational structure of the K+ complex
    • Suwan S, Isobe M, Ohtani I, Agata N, Mori M, Ohta M. Structure of cereulide, a cyclic dodecadepsipeptide toxin from Bacillus cereus and studies on NMR characteristics of its alkali metal complexes including a conformational structure of the K+ complex. J. Chem. Soc. Perkin Trans. 1995; 1: 765-775.
    • (1995) J. Chem. Soc. Perkin Trans , vol.1 , pp. 765-775
    • Suwan, S.1    Isobe, M.2    Ohtani, I.3    Agata, N.4    Mori, M.5    Ohta, M.6
  • 15
    • 39049110095 scopus 로고    scopus 로고
    • Polydiscamides B-D from a marine sponge Ircinia sp. as Potent human sensory neuron-specific G protein coupled receptor agonists
    • Feng Y, Carroll AR, Pass DM, Archbold JK, Avery VM, Quinn RJ. Polydiscamides B-D from a marine sponge Ircinia sp. as Potent human sensory neuron-specific G protein coupled receptor agonists. J. Nat. Prod. 2008; 71: 8-11.
    • (2008) J. Nat. Prod , vol.71 , pp. 8-11
    • Feng, Y.1    Carroll, A.R.2    Pass, D.M.3    Archbold, J.K.4    Avery, V.M.5    Quinn, R.J.6
  • 16
    • 0034969013 scopus 로고    scopus 로고
    • Somamides A and B, two new depsipeptide analogues of dolastatin 13 from a Fijian cyanobacterial assemblage of Lyngbya majuscula and Schizothrix species
    • Nogle LM, Williamson RT, Gerwick WH. Somamides A and B, two new depsipeptide analogues of dolastatin 13 from a Fijian cyanobacterial assemblage of Lyngbya majuscula and Schizothrix species. J. Nat. Prod. 2001; 64: 716-719.
    • (2001) J. Nat. Prod , vol.64 , pp. 716-719
    • Nogle, L.M.1    Williamson, R.T.2    Gerwick, W.H.3
  • 17
    • 65649142925 scopus 로고    scopus 로고
    • Micropeptins from the Freshwater cyanobacterium Microcystis aeruginosa (NIES-100)
    • Kisugi T, Okino T. Micropeptins from the Freshwater cyanobacterium Microcystis aeruginosa (NIES-100). J. Nat. Prod. 2009; 72: 777-781.
    • (2009) J. Nat. Prod , vol.72 , pp. 777-781
    • Kisugi, T.1    Okino, T.2
  • 18
    • 0033612125 scopus 로고    scopus 로고
    • Oscillapeptins A to F, serine protease inhibitors from the three strains of Oscillatoria agardhii
    • Itou Y, Ishida K, Shin HJ, Murakami M. Oscillapeptins A to F, serine protease inhibitors from the three strains of Oscillatoria agardhii. Tetrahedron 1999; 55: 6871-6882.
    • (1999) Tetrahedron , vol.55 , pp. 6871-6882
    • Itou, Y.1    Ishida, K.2    Shin, H.J.3    Murakami, M.4
  • 19
    • 33746866335 scopus 로고    scopus 로고
    • Cytoskeleton alterations induced by Geodia corticostylifera depsipeptides in breast cancer cells
    • Rangel M, Prado MP, Konno K, Naoki H, Freitas JC, Machado-Santelli GM. Cytoskeleton alterations induced by Geodia corticostylifera depsipeptides in breast cancer cells. Peptides 2006; 27: 2047-2057.
    • (2006) Peptides , vol.27 , pp. 2047-2057
    • Rangel, M.1    Prado, M.P.2    Konno, K.3    Naoki, H.4    Freitas, J.C.5    Machado-Santelli, G.M.6
  • 22
    • 0037179166 scopus 로고    scopus 로고
    • Isolation of callipeltins A-C and of two new open-chain derivatives of callipeltin A from the marine sponge Latrunculia sp. A revision of the stereostructure of callipeltins
    • Zampella A, Randazzo A, Borbone N, Luciani S, Trevisi L, Debitus C, D'Auria MV. Isolation of callipeltins A-C and of two new open-chain derivatives of callipeltin A from the marine sponge Latrunculia sp. A revision of the stereostructure of callipeltins. Tetrahedron Lett. 2002; 43: 6163-6166.
    • (2002) Tetrahedron Lett , vol.43 , pp. 6163-6166
    • Zampella, A.1    Randazzo, A.2    Borbone, N.3    Luciani, S.4    Trevisi, L.5    Debitus, C.6    D'Auria, M.V.7
  • 23
    • 65549150450 scopus 로고    scopus 로고
    • A convergent synthesis of the proposed structure of antitumor depsipeptide stereocalpin A
    • Ghosh AK, Xu C-X. A convergent synthesis of the proposed structure of antitumor depsipeptide stereocalpin A. Org. Lett. 2009; 11: 1963-1966.
    • (2009) Org. Lett , vol.11 , pp. 1963-1966
    • Ghosh, A.K.1    Xu, C.-X.2
  • 24
    • 60849089353 scopus 로고    scopus 로고
    • Celebesides A-C and theopapuamides B-D, depsipeptides from an Indonesian sponge that inhibit HIV-1 entry
    • Plaza A, Bifulco G, Keffer JL, Lloyd JR, Baker HL, Bewley CA. Celebesides A-C and theopapuamides B-D, depsipeptides from an Indonesian sponge that inhibit HIV-1 entry. J. Org.Chem. 2009; 74: 504-512.
    • (2009) J. Org.Chem , vol.74 , pp. 504-512
    • Plaza, A.1    Bifulco, G.2    Keffer, J.L.3    Lloyd, J.R.4    Baker, H.L.5    Bewley, C.A.6
  • 25
    • 0033996619 scopus 로고    scopus 로고
    • Yanucamides A and B, two new depsipeptides froman assemblage of themarine cyanobacteria Lyngbya majuscula and Schizothrix species
    • Sitachitta N, Williamson RT, Gerwick WH. Yanucamides A and B, two new depsipeptides froman assemblage of themarine cyanobacteria Lyngbya majuscula and Schizothrix species. J. Nat. Prod. 2000; 63: 197-200.
    • (2000) J. Nat. Prod , vol.63 , pp. 197-200
    • Sitachitta, N.1    Williamson, R.T.2    Gerwick, W.H.3
  • 26
    • 0033572757 scopus 로고    scopus 로고
    • Total synthesis and comparative evaluation of luzopeptin A-C and quinoxapeptin A-C
    • Boger DL, Ledeboer MW, Kume M, Searcey M, Jin Q. Total synthesis and comparative evaluation of luzopeptin A-C and quinoxapeptin A-C. J. Am. Chem. Soc. 1999; 121: 11375-11383.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 11375-11383
    • Boger, D.L.1    Ledeboer, M.W.2    Kume, M.3    Searcey, M.4    Jin, Q.5
  • 27
    • 60549092554 scopus 로고    scopus 로고
    • Hantupeptin A, a cytotoxic cyclic cepsipeptide from a singapore collection of Lyngbya majuscule
    • Tripathi A, Puddick J, PrinsepMR, Lee PPF, Lik TT. Hantupeptin A, a cytotoxic cyclic cepsipeptide from a singapore collection of Lyngbya majuscule. J. Nat. Prod. 2009; 72: 29-32.
    • (2009) J. Nat. Prod , vol.72 , pp. 29-32
    • Tripathi, A.1    Puddick, J.2    Prinsep, M.R.3    Lee, P.P.F.4    Lik, T.T.5
  • 28
    • 0033961890 scopus 로고    scopus 로고
    • Tamandarins A and B: New cytotoxic depsipeptides from a Brazilian ascidian of the family didemnidae
    • Vervoort H, Fenical W, Epifanio RDA. Tamandarins A and B: new cytotoxic depsipeptides from a Brazilian ascidian of the family didemnidae. J. Org. Chem. 2000; 65: 782-792.
    • (2000) J. Org. Chem , vol.65 , pp. 782-792
    • Vervoort, H.1    Fenical, W.2    Epifanio, R.D.A.3
  • 30
    • 33749568589 scopus 로고    scopus 로고
    • Solution structures by NMR of a novel antifungal drug: Petriellin A
    • Dang J, Aurelio L, Hughes AB, Brownlee RTC. Solution structures by NMR of a novel antifungal drug: petriellin A. Org. Biomol. Chem. 2006; 4: 3802-3807.
    • (2006) Org. Biomol. Chem , vol.4 , pp. 3802-3807
    • Dang, J.1    Aurelio, L.2    Hughes, A.B.3    Brownlee, R.T.C.4
  • 32
    • 58149161563 scopus 로고    scopus 로고
    • Gunasekera SP, Ritson-Williams R, Paul VJ. Carriebowmide, a new cyclodepsipeptide from the marine cyanobacterium Lyngbya polychroa. J. Nat. Prod. 2008; 71: 2060-2063.
    • Gunasekera SP, Ritson-Williams R, Paul VJ. Carriebowmide, a new cyclodepsipeptide from the marine cyanobacterium Lyngbya polychroa. J. Nat. Prod. 2008; 71: 2060-2063.
  • 33
    • 43649092033 scopus 로고    scopus 로고
    • Cytotoxicities of enniatins H, I, and MK1688 from Fusarium oxysporum KFCC 11363P
    • Lee H-S, Song H-H, Jeong J-H, Shin C-G, Choi S-U, Lee C. Cytotoxicities of enniatins H, I, and MK1688 from Fusarium oxysporum KFCC 11363P. Toxicon 2008; 51: 1178-1185.
    • (2008) Toxicon , vol.51 , pp. 1178-1185
    • Lee, H.-S.1    Song, H.-H.2    Jeong, J.-H.3    Shin, C.-G.4    Choi, S.-U.5    Lee, C.6
  • 34
    • 60349090957 scopus 로고    scopus 로고
    • In vitro synthesis of new cyclodepsipeptides of the PF1022-type: Probing the α-D-hydroxy acid tolerance of PF1022 synthetase
    • Müller J, Feifel SC, Schmiederer T, Zocher R, Süssmuth RD. In vitro synthesis of new cyclodepsipeptides of the PF1022-type: probing the α-D-hydroxy acid tolerance of PF1022 synthetase. ChemBioChem 2009; 10: 323-328.
    • (2009) ChemBioChem , vol.10 , pp. 323-328
    • Müller, J.1    Feifel, S.C.2    Schmiederer, T.3    Zocher, R.4    Süssmuth, R.D.5
  • 37
    • 0033030761 scopus 로고    scopus 로고
    • Unique molecular conformation of aureobasidin A, a highly amide N-methylated cyclic depsipeptide with potent antifungal activity: X-ray crystal structure andmolecular modeling studies
    • In Y, Ishida T, Takesako K. Unique molecular conformation of aureobasidin A, a highly amide N-methylated cyclic depsipeptide with potent antifungal activity: X-ray crystal structure andmolecular modeling studies. J. Peptide Res. 1999; 53: 492-500.
    • (1999) J. Peptide Res , vol.53 , pp. 492-500
    • In, Y.1    Ishida, T.2    Takesako, K.3
  • 38
    • 0027763468 scopus 로고
    • Isolation, structure, and synthesis of dolastatin D, a cytotoxic cyclic depsipeptide from the sea hare Dolabella auricularia
    • Sone H, Nemoto T, Ishiwata H, Ojika M, Yamada K. Isolation, structure, and synthesis of dolastatin D, a cytotoxic cyclic depsipeptide from the sea hare Dolabella auricularia. Tetrahedron Lett. 1993; 34: 8449-8452.
    • (1993) Tetrahedron Lett , vol.34 , pp. 8449-8452
    • Sone, H.1    Nemoto, T.2    Ishiwata, H.3    Ojika, M.4    Yamada, K.5
  • 40
    • 17444405602 scopus 로고    scopus 로고
    • The wewakpeptins, cyclic depsipeptides from a Papua New Guinea collection of the marine cyanobacterium Lyngbya semiplena
    • Han B, Goeger D, Maier CS, Gerwick WH. The wewakpeptins, cyclic depsipeptides from a Papua New Guinea collection of the marine cyanobacterium Lyngbya semiplena. J. Org. Chem. 2005; 70: 3133-3139.
    • (2005) J. Org. Chem , vol.70 , pp. 3133-3139
    • Han, B.1    Goeger, D.2    Maier, C.S.3    Gerwick, W.H.4
  • 41
    • 0016106566 scopus 로고
    • Theoretical conformational analysis of randomly coiling and ordered depsipetide chains
    • Ingwall RT, Goodman M. Polydepsipeptides. III. Theoretical conformational analysis of randomly coiling and ordered depsipetide chains. Macromolecules 1974; 7: 598-605.
    • (1974) Macromolecules , vol.7 , pp. 598-605
    • Ingwall, R.T.1    Goodman, M.2
  • 42
    • 0017003821 scopus 로고
    • 5. Experimental conformational analysis of poly(l-alanyl-l-lactic acid) and related model compounds
    • Ingwall RT, Gilon C, Goodman M. Polydepsipeptides. 5. Experimental conformational analysis of poly(l-alanyl-l-lactic acid) and related model compounds. Macromolecules 1976; 9: 802-808.
    • (1976) Macromolecules , vol.9 , pp. 802-808
    • Ingwall, R.T.1    Gilon, C.2    Goodman, M.3    Polydepsipeptides4
  • 43
    • 84962393635 scopus 로고    scopus 로고
    • Molecular modeling of conformational properties of oligodepsipeptides
    • Zhang J, King M, Suggs L, Ren P. Molecular modeling of conformational properties of oligodepsipeptides. Biomacromolecules 2007; 8: 3015-3024.
    • (2007) Biomacromolecules , vol.8 , pp. 3015-3024
    • Zhang, J.1    King, M.2    Suggs, L.3    Ren, P.4
  • 44
    • 49349103899 scopus 로고    scopus 로고
    • Conformational preferences and cis-trans isomerization of L-lactic acid residue
    • Kang YK, Byun BJ. Conformational preferences and cis-trans isomerization of L-lactic acid residue. J. Phys. Chem. B 2008; 112: 9126-9134.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 9126-9134
    • Kang, Y.K.1    Byun, B.J.2
  • 45
    • 76749129193 scopus 로고    scopus 로고
    • URL: www.ccdc.cam.ac.uk The Cambridge Structural Database CSD version 5.30 (November 2008).
    • URL: www.ccdc.cam.ac.uk The Cambridge Structural Database CSD version 5.30 (November 2008).
  • 46
    • 76749142290 scopus 로고    scopus 로고
    • URL: http://www.chem.qmul.ac.uk/iupac/AminoAcid (3AA-19.7. Peptide Analogues).
    • URL: http://www.chem.qmul.ac.uk/iupac/AminoAcid (3AA-19.7. Peptide Analogues).
  • 47
    • 76749129490 scopus 로고    scopus 로고
    • Frisch MJ, Trucks GW, Schlegel HB, Scuseria GE, Robb MA, Chesseman JR, Montgomery Jr JA, Vreven T, Kudin KN, Burant JC, Millam JM, Iyengar SS, Tomasi J, Barone V, Mennucci B, Cossi M, Scalmani G, Rega N, Petersson GA, Nakatsuji H, Hada M, Ehara M, Toyota K, Fukuda R, Hasegawa J, Ishida M, Nakajima T, Honda Y, Kitao O, Nakai H, Klene M, LiX, Knox JE, Hratchnian HP, Cross JB, Adamo C, Jaramillo J, Gomperts R, Stratmann RE, Yazyev O, Austin AJ, Cammi R, Pomelli C, Ochterski JW, Ayala PY, Morokuma K, Voth GA, Salvador P, Dannenberg JJ, Zakrzewski VG, Dapprich S, Danields AD, Strain MC, Farkas O, Malick DK, Rabuck AD, Raghavachari K, Foresman JB, Ortiz JV, Cui Q, Baboul AG, Clifford S, Cioslowski J, Stefanov J, Liu G, Liashenko A, Piskorz P, Komaromi I, Martin RL, Fox DJ, Keith T, Al-Laham MA, Peng CY, Nanayakkara A, Challacombe M, Gill PMW, Johnson B, Chen W, Wong MW, Gonzalex C, Pople JA. Gaussian'03 Revision C.02, Gaussian Inc, Pittsburgh, PA; 2003
    • Frisch MJ, Trucks GW, Schlegel HB, Scuseria GE, Robb MA, Chesseman JR, Montgomery Jr JA, Vreven T, Kudin KN, Burant JC, Millam JM, Iyengar SS, Tomasi J, Barone V, Mennucci B, Cossi M, Scalmani G, Rega N, Petersson GA, Nakatsuji H, Hada M, Ehara M, Toyota K, Fukuda R, Hasegawa J, Ishida M, Nakajima T, Honda Y, Kitao O, Nakai H, Klene M, LiX, Knox JE, Hratchnian HP, Cross JB, Adamo C, Jaramillo J, Gomperts R, Stratmann RE, Yazyev O, Austin AJ, Cammi R, Pomelli C, Ochterski JW, Ayala PY, Morokuma K, Voth GA, Salvador P, Dannenberg JJ, Zakrzewski VG, Dapprich S, Danields AD, Strain MC, Farkas O, Malick DK, Rabuck AD, Raghavachari K, Foresman JB, Ortiz JV, Cui Q, Baboul AG, Clifford S, Cioslowski J, Stefanov J, Liu G, Liashenko A, Piskorz P, Komaromi I, Martin RL, Fox DJ, Keith T, Al-Laham MA, Peng CY, Nanayakkara A, Challacombe M, Gill PMW, Johnson B, Chen W, Wong MW, Gonzalex C, Pople JA. Gaussian'03 Revision C.02, Gaussian Inc.: Pittsburgh, PA; 2003.
  • 48
    • 84962432699 scopus 로고
    • Approximate evaluations of the electrostatic free energy and internal energy changes in solution processes
    • Miertus S, Tomasi J. Approximate evaluations of the electrostatic free energy and internal energy changes in solution processes. Chem. Phys. 1982; 65: 239-245.
    • (1982) Chem. Phys , vol.65 , pp. 239-245
    • Miertus, S.1    Tomasi, J.2
  • 49
    • 84961980477 scopus 로고    scopus 로고
    • Quantum mechanical continuum salvationmodels
    • Tomasi J, Mennucci B, Cammi R. Quantum mechanical continuum salvationmodels. Chem. Rev. 2005; 105: 2999-3093.
    • (2005) Chem. Rev , vol.105 , pp. 2999-3093
    • Tomasi, J.1    Mennucci, B.2    Cammi, R.3
  • 50
    • 0037018526 scopus 로고    scopus 로고
    • Conformational study of the alanine dipeptide at the MP2 and DFT levels
    • Vargas R, Garza J, Hay BP, Dixon DA. Conformational study of the alanine dipeptide at the MP2 and DFT levels. J. Phys. Chem. A 2002; 106: 3213-3218.
    • (2002) J. Phys. Chem. A , vol.106 , pp. 3213-3218
    • Vargas, R.1    Garza, J.2    Hay, B.P.3    Dixon, D.A.4
  • 51
    • 0037441653 scopus 로고    scopus 로고
    • Lovell SC, Davis IW, Arendall III WB, de Bakker PIW, Word JM, Prisant MG, Richardson JS, Richardson DC. Structure Validation by Cα Geometry: φ,ψ and Cβ Deviation. PROTEINS: Structure, Function, and Genetics 2003; 50: 437-450.
    • Lovell SC, Davis IW, Arendall III WB, de Bakker PIW, Word JM, Prisant MG, Richardson JS, Richardson DC. Structure Validation by Cα Geometry: φ,ψ and Cβ Deviation. PROTEINS: Structure, Function, and Genetics 2003; 50: 437-450.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.