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Volumn 128, Issue 1, 2011, Pages 25-37

Computational insight into protein circular dichroism: Detailed analysis of contributions of individual chromophores in TEM-1 β-lactamase

Author keywords

Aromatic and disulfide chromophores; Beta lactamase; Circular dichroism; Matrix method

Indexed keywords


EID: 79251623123     PISSN: 1432881X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00214-010-0744-4     Document Type: Article
Times cited : (9)

References (42)
  • 1
    • 34249686052 scopus 로고    scopus 로고
    • Application of electronic circular dichroism in configurational and conformational analysis of organic compounds
    • Berova N, Di Bari L, Pescitelli G (2007) Application of electronic circular dichroism in configurational and conformational analysis of organic compounds. Chem Soc Rev 36: 914-931.
    • (2007) Chem Soc Rev , vol.36 , pp. 914-931
    • Berova, N.1    Di Bari, L.2    Pescitelli, G.3
  • 4
    • 0036965576 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism and conventional circular dichroism spectroscopy: a comparison
    • Lees JG, Wallace BA (2002) Synchrotron radiation circular dichroism and conventional circular dichroism spectroscopy: a comparison. Spectroscopy 16: 121-125.
    • (2002) Spectroscopy , vol.16 , pp. 121-125
    • Lees, J.G.1    Wallace, B.A.2
  • 5
    • 0018339835 scopus 로고
    • The interpretaion of near-ultraviolet circular dichroism
    • Kahn PC (1979) The interpretaion of near-ultraviolet circular dichroism. Methods Enzymol 61: 339.
    • (1979) Methods Enzymol , vol.61 , pp. 339
    • Kahn, P.C.1
  • 7
    • 33644873189 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism spectroscopy of proteins and applications in structural and functional genomics
    • Miles AJ, Wallace BA (2006) Synchrotron radiation circular dichroism spectroscopy of proteins and applications in structural and functional genomics. Chem Soc Rev 35(1): 39-51.
    • (2006) Chem Soc Rev , vol.35 , Issue.1 , pp. 39-51
    • Miles, A.J.1    Wallace, B.A.2
  • 8
    • 67949124581 scopus 로고    scopus 로고
    • Interactions of a tetraanionic porphyrin with DNA: from a Z-DNA sensor to a versatile supramolecular device
    • D'Urso A, Mammana A, Balaz M, Holmes AE, Berova N, Lauceri R, Purrello R (2009) Interactions of a tetraanionic porphyrin with DNA: from a Z-DNA sensor to a versatile supramolecular device. J Am Chem Soc 131: 2046-2047.
    • (2009) J Am Chem Soc , vol.131 , pp. 2046-2047
    • D'Urso, A.1    Mammana, A.2    Balaz, M.3    Holmes, A.E.4    Berova, N.5    Lauceri, R.6    Purrello, R.7
  • 9
    • 56349098780 scopus 로고    scopus 로고
    • Chiral sulfinates studied by optical rotation, ECD and VCD: the absolute configuration of a cruciferous phytoalexin brassicanal C
    • Taniguchi T, Monde K, Nakanishi K, Berova N (2008) Chiral sulfinates studied by optical rotation, ECD and VCD: the absolute configuration of a cruciferous phytoalexin brassicanal C. Organ Biomol Chem 6: 4399-4405.
    • (2008) Organ Biomol Chem , vol.6 , pp. 4399-4405
    • Taniguchi, T.1    Monde, K.2    Nakanishi, K.3    Berova, N.4
  • 11
    • 0031923940 scopus 로고    scopus 로고
    • Beta-lactamases as models for protein-folding studies
    • Vanhove M, Lejeune A, Pain RH (1998) Beta-lactamases as models for protein-folding studies. Cell Mol Life Sci 54: 372-377.
    • (1998) Cell Mol Life Sci , vol.54 , pp. 372-377
    • Vanhove, M.1    Lejeune, A.2    Pain, R.H.3
  • 12
    • 79251608048 scopus 로고    scopus 로고
    • PhD Thesis, PhD, Bulgarian Academy of Sciences, Sofia
    • Christov C (2002) PhD Thesis, PhD, Bulgarian Academy of Sciences, Sofia.
    • (2002)
    • Christov, C.1
  • 13
    • 0039894210 scopus 로고    scopus 로고
    • Calculation of the CD spectrum of class A beta-lactamase from Escherichia coli (TEM-1)
    • Christov C, Gabriel S, Atanasov B, Fleischhauer J (2001) Calculation of the CD spectrum of class A beta-lactamase from Escherichia coli (TEM-1). Z Naturforsch A 56: 757-760.
    • (2001) Z Naturforsch , vol.A 56 , pp. 757-760
    • Christov, C.1    Gabriel, S.2    Atanasov, B.3    Fleischhauer, J.4
  • 14
    • 7044256879 scopus 로고    scopus 로고
    • Mechanisms of generation of rotational strengths in TEM-1 beta-lactamase.Part I: theoretical analysis of the influences of conformational changes in the near-UV
    • Christov C, Karabencheva T (2004) Mechanisms of generation of rotational strengths in TEM-1 beta-lactamase. Part I: theoretical analysis of the influences of conformational changes in the near-UV. Chem Phys Lett 396: 282-287.
    • (2004) Chem Phys Lett , vol.396 , pp. 282-287
    • Christov, C.1    Karabencheva, T.2
  • 15
    • 10344237532 scopus 로고    scopus 로고
    • Mechanisms of generation of the rotational strengths in TEM-1 β-Lactamase Part II: theoretical study of the effects of the electrostatic interactions in the near-UV
    • Christov C, Kantardjiev A, Karabencheva T, Tielens F (2004) Mechanisms of generation of the rotational strengths in TEM-1 ß-Lactamase Part II: theoretical study of the effects of the electrostatic interactions in the near-UV. Chem Phys Lett 400: 524-530.
    • (2004) Chem Phys Lett , vol.400 , pp. 524-530
    • Christov, C.1    Kantardjiev, A.2    Karabencheva, T.3    Tielens, F.4
  • 16
    • 43249098735 scopus 로고    scopus 로고
    • Relationship between chiroptical properties, structural changes and interactions in enzymes: a computational study on beta-lactamases from class A
    • Christov C, Karabencheva T, Lodola A (2008) Relationship between chiroptical properties, structural changes and interactions in enzymes: a computational study on beta-lactamases from class A. Comput Biol Chem 32: 167-175.
    • (2008) Comput Biol Chem , vol.32 , pp. 167-175
    • Christov, C.1    Karabencheva, T.2    Lodola, A.3
  • 17
    • 41749089998 scopus 로고    scopus 로고
    • Aromatic interactions and rotational strengths within protein environment: an electronic structural study on beta-lactamases from class A
    • Christov C, Karabencheva T, Lodola A (2008) Aromatic interactions and rotational strengths within protein environment: an electronic structural study on beta-lactamases from class A. Chem Phys Lett 456: 89-95.
    • (2008) Chem Phys Lett , vol.456 , pp. 89-95
    • Christov, C.1    Karabencheva, T.2    Lodola, A.3
  • 19
    • 0027275788 scopus 로고
    • Crystal-structure of Escherichia coli Tem1 Beta-lactamase at 1.8-Angstrom resolution
    • Jelsch C, Mourey L, Masson JM, Samama JP (1993) Crystal-structure of Escherichia coli Tem1 Beta-lactamase at 1. 8-Angstrom resolution. Proteins 16: 364-383.
    • (1993) Proteins , vol.16 , pp. 364-383
    • Jelsch, C.1    Mourey, L.2    Masson, J.M.3    Samama, J.P.4
  • 20
    • 0029738864 scopus 로고    scopus 로고
    • Crystal structure of 6 alpha-(hydroxymethyl)penicillanate complexed to the TEM-1 beta-lactamase from Escherichia coli: evidence on the mechanism of action of a novel inhibitor designed by a computer-aided process
    • Maveyraud L, Massova I, Birck C, Miyashita K, Samama JP, Mobashery S (1996) Crystal structure of 6 alpha-(hydroxymethyl)penicillanate complexed to the TEM-1 beta-lactamase from Escherichia coli: evidence on the mechanism of action of a novel inhibitor designed by a computer-aided process. J Am Chem Soc 118: 7435-7440.
    • (1996) J Am Chem Soc , vol.118 , pp. 7435-7440
    • Maveyraud, L.1    Massova, I.2    Birck, C.3    Miyashita, K.4    Samama, J.P.5    Mobashery, S.6
  • 21
    • 0032581949 scopus 로고    scopus 로고
    • Structural basis for clinical longevity of carbapenem antibiotics in the face of challenge by the common class A beta-lactamases from the antibiotic-resistant bacteria
    • Maveyraud L, Mourey L, Kotra LP, Pedelacq JD, Guillet V, Mobashery S, Samama JP (1998) Structural basis for clinical longevity of carbapenem antibiotics in the face of challenge by the common class A beta-lactamases from the antibiotic-resistant bacteria. J Am Chem Soc 120: 9748-9752.
    • (1998) J Am Chem Soc , vol.120 , pp. 9748-9752
    • Maveyraud, L.1    Mourey, L.2    Kotra, L.P.3    Pedelacq, J.D.4    Guillet, V.5    Mobashery, S.6    Samama, J.P.7
  • 22
    • 0032562183 scopus 로고    scopus 로고
    • Crystal structure of an acylation transition-state analog of the TEM-1 beta-lactamase. Mechanistic implications for class A beta-lactamases
    • Maveyraud L, Pratt RF, Samama JP (1998) Crystal structure of an acylation transition-state analog of the TEM-1 beta-lactamase. Mechanistic implications for class A beta-lactamases. Biochemistry 37: 2622-2628.
    • (1998) Biochemistry , vol.37 , pp. 2622-2628
    • Maveyraud, L.1    Pratt, R.F.2    Samama, J.P.3
  • 23
  • 25
    • 36849127374 scopus 로고
    • Theory of one-electron rotatory power
    • Condon EU (1937) Theory of one-electron rotatory power. J Chem Phys 5: 753.
    • (1937) J Chem Phys , vol.5 , pp. 753
    • Condon, E.U.1
  • 26
    • 37049170445 scopus 로고
    • The physical significance of optical rotatory power
    • Kuhn W (1930) The physical significance of optical rotatory power. Trans Faraday Soc 46: 293-308.
    • (1930) Trans Faraday Soc , vol.46 , pp. 293-308
    • Kuhn, W.1
  • 27
    • 36849120258 scopus 로고
    • On the theory of optical rotatory power
    • Kirkwood JG (1937) On the theory of optical rotatory power. J Chem Phys 5: 479-491.
    • (1937) J Chem Phys , vol.5 , pp. 479-491
    • Kirkwood, J.G.1
  • 28
    • 0000147704 scopus 로고
    • Critique on the theory of optical activity of helical polymers
    • Moffitt W, FItts DD, Kirkwood JG (1957) Critique on the theory of optical activity of helical polymers. Proc Natl Acad Sci USA 43: 723-730.
    • (1957) Proc Natl Acad Sci USA , vol.43 , pp. 723-730
    • Moffitt, W.1    Fitts, D.D.2    Kirkwood, J.G.3
  • 29
    • 33947321475 scopus 로고
    • Symmetry rules for optical rotation
    • Schellman J (1968) Symmetry rules for optical rotation. Acc Chem Res 1: 144-151.
    • (1968) Acc Chem Res , vol.1 , pp. 144-151
    • Schellman, J.1
  • 30
    • 0014448179 scopus 로고
    • Rotatory properties of molecules containing two peptide groups: theory
    • Bayley PM, Nielsen EB, Schellman JA (1969) Rotatory properties of molecules containing two peptide groups: theory. J Phys Chem 73: 228-243.
    • (1969) J Phys Chem , vol.73 , pp. 228-243
    • Bayley, P.M.1    Nielsen, E.B.2    Schellman, J.A.3
  • 32
    • 0000291490 scopus 로고
    • Chiroptical properties of proteins. 1. Near-ultraviolet circular-dichroism of ribonuclease-S
    • Goux WJ, Hooker TM (1980) Chiroptical properties of proteins. 1. Near-ultraviolet circular-dichroism of ribonuclease-S. J Am Chem Soc 102: 7080-7087.
    • (1980) J Am Chem Soc , vol.102 , pp. 7080-7087
    • Goux, W.J.1    Hooker, T.M.2
  • 35
    • 79251630044 scopus 로고
    • Ph. D. thesis, RWTH, Aachen
    • Kramer B (1991) Ph. D. thesis, RWTH, Aachen.
    • (1991)
    • Kramer, B.1
  • 37
    • 33947297954 scopus 로고
    • Photochemistry of the model phototropic system involving flavines and indoles. III. A spectroscopic study of the polarized luminescence of indoles
    • Song PS, Kurtin WE (1969) Photochemistry of the model phototropic system involving flavines and indoles. III. A spectroscopic study of the polarized luminescence of indoles. J Am Chem Soc 91: 4892-4906.
    • (1969) J Am Chem Soc , vol.91 , pp. 4892-4906
    • Song, P.S.1    Kurtin, W.E.2
  • 38
    • 0001688829 scopus 로고
    • Excited-state properties of the indole chromophore-electronic-transition moment directions from linear dichroism measurements-effect of methyl and methoxy substituents
    • Albinsson B, Norden B (1992) Excited-state properties of the indole chromophore-electronic-transition moment directions from linear dichroism measurements-effect of methyl and methoxy substituents. J Phys Chem 96: 6204-6212.
    • (1992) J Phys Chem , vol.96 , pp. 6204-6212
    • Albinsson, B.1    Norden, B.2
  • 40
    • 0034697986 scopus 로고    scopus 로고
    • What can disulfide bonds tell us about protein energetics, function and folding: simulations and biinformatics analysis
    • Abkevich VI, Shakhnovich EI (2000) What can disulfide bonds tell us about protein energetics, function and folding: simulations and biinformatics analysis. J Mol Biol 300: 975-985.
    • (2000) J Mol Biol , vol.300 , pp. 975-985
    • Abkevich, V.I.1    Shakhnovich, E.I.2
  • 42
    • 41449118757 scopus 로고    scopus 로고
    • Structure and mechanisms of the DsbB-DsbA disulfide bond generation machine
    • Inaba K, Ito K (2008) Structure and mechanisms of the DsbB-DsbA disulfide bond generation machine. Biochimica Biophysica Acta-Mole Cell Res 1783: 520-529.
    • (2008) Biochimica Biophysica Acta-Mole Cell Res , vol.1783 , pp. 520-529
    • Inaba, K.1    Ito, K.2


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