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Volumn 117, Issue 9, 2013, Pages 2645-2652

Vibrational circular dichroism spectra of lysozyme solutions: Solvent effects on thermal denaturation processes

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; AGGREGATES; DENATURATION; DEUTERIUM; DICHROISM; SOLVENTS;

EID: 84875011266     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp311268x     Document Type: Article
Times cited : (25)

References (49)
  • 1
    • 72949120004 scopus 로고    scopus 로고
    • Influence of Glycerol on the Structure and Thermal Stability of Lysozyme: A Dynamic Light Scattering and Circular Dichroism Study
    • Esposito, A.; Comez, L.; Cinelli, S.; Scarponi, F.; Onori, G. Influence of Glycerol on the Structure and Thermal Stability of Lysozyme: a Dynamic Light Scattering and Circular Dichroism Study J. Phys. Chem. B 2009, 113, 16420-16424
    • (2009) J. Phys. Chem. B , vol.113 , pp. 16420-16424
    • Esposito, A.1    Comez, L.2    Cinelli, S.3    Scarponi, F.4    Onori, G.5
  • 2
    • 33646927210 scopus 로고    scopus 로고
    • Protein-solvent interactions
    • DOI 10.1021/cr040437f
    • Prabhu, N.; Sharp, K. Protein-Solvent Interactions Chem. Rev. 2006, 106, 1616-1623 (Pubitemid 43792774)
    • (2006) Chemical Reviews , vol.106 , Issue.5 , pp. 1616-1623
    • Prabhu, N.1    Sharp, K.2
  • 3
    • 0142049584 scopus 로고    scopus 로고
    • Water and Cellular Folding Processes
    • Csermely, P. Water and Cellular Folding Processes Cell. Mol. Biol. 2001, 47, 791-800
    • (2001) Cell. Mol. Biol. , vol.47 , pp. 791-800
    • Csermely, P.1
  • 4
    • 4644320684 scopus 로고    scopus 로고
    • Simultaneous determination of structural and thermodynamic effects of carbohydrate solutes on the thermal stability of ribonuclease A
    • DOI 10.1021/ja0481777
    • O'Connor, T. F.; Debenedetti, P. G.; Carbeck, J. D. Simultaneous Determination of Structural and Thermodynamic Effects of Carbohydrate Solutes on the Thermal Stability of Ribonuclease A J. Am. Chem. Soc. 2004, 126, 11794-11795 (Pubitemid 39298319)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.38 , pp. 11794-11795
    • O'Connor, T.F.1    Debenedetti, P.G.2    Carbeck, J.D.3
  • 5
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding and aggregation
    • DOI 10.1016/j.semcdb.2003.12.008
    • Dobson, C. M. Principles of Protein Folding, Misfolding and Aggregation Semin. Cell Dev. Biol. 2004, 15, 3-16 (Pubitemid 38177363)
    • (2004) Seminars in Cell and Developmental Biology , vol.15 , Issue.1 , pp. 3-16
    • Dobson, C.M.1
  • 8
    • 0033018671 scopus 로고    scopus 로고
    • Vibrational circular dichroism spectroscopy of selected oligopeptide conformations
    • DOI 10.1016/S0968-0896(98)00217-X, PII S096808969800217X
    • Keiderling, T. A.; Silva, R. A.; Yoder, G.; Dukor, R. K. Vibrational Circular Dichroism Spectroscopy of Selected Oligopeptide Conformations Bioorg. Med. Chem. 1999, 7, 133-141 (Pubitemid 29097701)
    • (1999) Bioorganic and Medicinal Chemistry , vol.7 , Issue.1 , pp. 133-141
    • Keiderling, T.A.1    Silva, R.A.G.D.2    Yoder, G.3    Dukor, R.K.4
  • 9
    • 0028700904 scopus 로고
    • Empirical Studies of Protein Secondary Structure by Vibrational Circular Dichroism and Related Techniques. A -Lactalbumin and Lysozyme as Examples
    • Keiderling, T. A.; Wang, B.; Urbanova, M.; Pancoska, P.; Dukor, R. K. Empirical Studies of Protein Secondary Structure by Vibrational Circular Dichroism and Related Techniques. A -Lactalbumin and Lysozyme as Examples Faraday Discuss. 1994, 263-285
    • (1994) Faraday Discuss. , pp. 263-285
    • Keiderling, T.A.1    Wang, B.2    Urbanova, M.3    Pancoska, P.4    Dukor, R.K.5
  • 10
    • 77953832319 scopus 로고    scopus 로고
    • Near-Infrared and Mid-Infrared Fourier Transform Vibrational Circular Dichroism of Proteins in Aqueous Solution
    • Ma, S.; Freedman, T. B.; Dukor, R. K.; Nafie, L. A. Near-Infrared and Mid-Infrared Fourier Transform Vibrational Circular Dichroism of Proteins in Aqueous Solution Appl. Spectrosc. 2010, 64, 615-626
    • (2010) Appl. Spectrosc. , vol.64 , pp. 615-626
    • Ma, S.1    Freedman, T.B.2    Dukor, R.K.3    Nafie, L.A.4
  • 11
    • 0022780707 scopus 로고
    • Vibrational Circular Dichroism Spectra of Three Conformationally Distinct States and an Unordered State of Poly(L-Lysine) in Deuterated Aqueous Solution
    • Paterlini, M. G.; Freedman, T. B.; Nafie, L. A. Vibrational Circular Dichroism Spectra of Three Conformationally Distinct States and an Unordered State of Poly(L-Lysine) in Deuterated Aqueous Solution Biopolymers 1986, 25, 1751-1765
    • (1986) Biopolymers , vol.25 , pp. 1751-1765
    • Paterlini, M.G.1    Freedman, T.B.2    Nafie, L.A.3
  • 12
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • Chiti, F.; Dobson, C. M. Protein Misfolding, Functional Amyloid, and Human Disease Annu. Rev. Biochem. 2006, 75, 333-366 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 13
    • 3142514201 scopus 로고    scopus 로고
    • Protein Aggregation and Neurodegenerative Disease
    • Ross, C. A.; Poirier, M. A. Protein Aggregation and Neurodegenerative Disease Nat. Med. 2004, 10 (Suppl) S10-7
    • (2004) Nat. Med. , vol.10 , Issue.SUPPL. , pp. 10-17
    • Ross, C.A.1    Poirier, M.A.2
  • 14
    • 34547947641 scopus 로고    scopus 로고
    • Conversion of non-fibrillar β-sheet oligomers into amyloid fibrils in Alzheimer's disease amyloid peptide aggregation
    • DOI 10.1016/j.bbrc.2007.07.082, PII S0006291X07015707
    • Benseny-Cases, N.; Cocera, M.; Cladera, J. Conversion of Non-Fibrillar β-sheet Oligomers into Amyloid Fibrils in Alzheimer's Disease Amyloid Peptide Aggregation Biochem. Biophys. Res. Commun. 2007, 361, 916-921 (Pubitemid 47263455)
    • (2007) Biochemical and Biophysical Research Communications , vol.361 , Issue.4 , pp. 916-921
    • Benseny-Cases, N.1    Cocera, M.2    Cladera, J.3
  • 15
    • 79960151809 scopus 로고    scopus 로고
    • Unfolding and Aggregation of Lysozyme: A Thermodynamic and Kinetic Study by FTIR Spectroscopy
    • Sassi, P.; Giugliarelli, A.; Paolantoni, M.; Morresi, A.; Onori, G. Unfolding and Aggregation of Lysozyme: a Thermodynamic and Kinetic Study by FTIR Spectroscopy Biophys. Chem. 2011, 158, 46-53
    • (2011) Biophys. Chem. , vol.158 , pp. 46-53
    • Sassi, P.1    Giugliarelli, A.2    Paolantoni, M.3    Morresi, A.4    Onori, G.5
  • 16
    • 59349083966 scopus 로고    scopus 로고
    • Protein Aggregation Kinetics, Mechanism, and Curve-Fitting: A Review of the Literature
    • Morris, A. M.; Watzky, M. A.; Finke, R. G. Protein Aggregation Kinetics, Mechanism, and Curve-Fitting: a Review of the Literature Biochim. Biophys. Acta 2009, 1794, 375-397
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 375-397
    • Morris, A.M.1    Watzky, M.A.2    Finke, R.G.3
  • 17
    • 0034636977 scopus 로고    scopus 로고
    • Is Polyproline II Helix the Killer Conformation? A Raman Optical Activity Study of the Amyloidogenic Prefibrillar Intermediate of Human Lysozyme
    • Blanch, E. W.; Morozova-Roche, L. A.; Cochran, D. A.; Doig, A. J.; Hecht, L.; Barron, L. D. Is Polyproline II Helix the Killer Conformation? A Raman Optical Activity Study of the Amyloidogenic Prefibrillar Intermediate of Human Lysozyme J. Mol. Biol. 2000, 301, 553-563
    • (2000) J. Mol. Biol. , vol.301 , pp. 553-563
    • Blanch, E.W.1    Morozova-Roche, L.A.2    Cochran, D.A.3    Doig, A.J.4    Hecht, L.5    Barron, L.D.6
  • 18
    • 79851507329 scopus 로고    scopus 로고
    • Vibrational Circular Dichroism as a Probe of Fibrillogenesis: The Origin of the Anomalous Intensity Enhancement of Amyloid-like Fibrils
    • Measey, T. J.; Schweitzer-Stenner, R. Vibrational Circular Dichroism as a Probe of Fibrillogenesis: The Origin of the Anomalous Intensity Enhancement of Amyloid-like Fibrils J. Am. Chem. Soc. 2010, 133, 1066-1076
    • (2010) J. Am. Chem. Soc. , vol.133 , pp. 1066-1076
    • Measey, T.J.1    Schweitzer-Stenner, R.2
  • 20
    • 79952009092 scopus 로고    scopus 로고
    • Conformational Changes in the Unfolding Process of Lysozyme in Water and Ethanol/Water Solutions
    • Sassi, P.; Onori, G.; Giugliarelli, A.; Paolantoni, M.; Cinelli, S.; Morresi, A. Conformational Changes in the Unfolding Process of Lysozyme in Water and Ethanol/Water Solutions J. Mol. Liq. 2011, 159, 112-116
    • (2011) J. Mol. Liq. , vol.159 , pp. 112-116
    • Sassi, P.1    Onori, G.2    Giugliarelli, A.3    Paolantoni, M.4    Cinelli, S.5    Morresi, A.6
  • 21
    • 84865987109 scopus 로고    scopus 로고
    • Heat-Denatured Lysozyme Aggregation and Gelation As Revealed by Combined Dielectric Relaxation Spectroscopy and Light Scattering Measurements
    • Giugliarelli, A.; Sassi, P.; Paolantoni, M.; Onori, G.; Cametti, C. Heat-Denatured Lysozyme Aggregation and Gelation As Revealed by Combined Dielectric Relaxation Spectroscopy and Light Scattering Measurements J. Phys. Chem. B 2012, 116, 10779-10785
    • (2012) J. Phys. Chem. B , vol.116 , pp. 10779-10785
    • Giugliarelli, A.1    Sassi, P.2    Paolantoni, M.3    Onori, G.4    Cametti, C.5
  • 22
    • 62349120772 scopus 로고    scopus 로고
    • Preferential Solvation of Lysozyme by Dimethyl Sulfoxide in Binary Solutions of Water and Dimethyl Sulfoxide
    • Kamiyama, T.; Liu, H.; Kimura, T. Preferential Solvation of Lysozyme by Dimethyl Sulfoxide in Binary Solutions of Water and Dimethyl Sulfoxide J. Therm. Anal. Calorim. 2009, 95, 353-359
    • (2009) J. Therm. Anal. Calorim. , vol.95 , pp. 353-359
    • Kamiyama, T.1    Liu, H.2    Kimura, T.3
  • 23
    • 55249101197 scopus 로고    scopus 로고
    • Effect of Sulfoxides on the Thermal Denaturation of Hen Lysozyme: A Calorimetric and Raman Study
    • Torreggiani, A.; Di Foggia, M.; Manco, I.; De Maio, A.; Markarian, S. A.; Bonora, S. Effect of Sulfoxides on the Thermal Denaturation of Hen Lysozyme: A Calorimetric and Raman Study J. Mol. Struct. 2008, 891, 115-122
    • (2008) J. Mol. Struct. , vol.891 , pp. 115-122
    • Torreggiani, A.1    Di Foggia, M.2    Manco, I.3    De Maio, A.4    Markarian, S.A.5    Bonora, S.6
  • 24
    • 35748974824 scopus 로고    scopus 로고
    • Protein precipitation and denaturation by dimethyl sulfoxide
    • DOI 10.1016/j.bpc.2007.09.004, PII S0301462207002050
    • Arakawa, T.; Kita, Y.; Timasheff, S. N. Protein Precipitation and Denaturation by Dimethyl Sulfoxide Biophys. Chem. 2007, 131, 62-70 (Pubitemid 350047519)
    • (2007) Biophysical Chemistry , vol.131 , Issue.1-3 , pp. 62-70
    • Arakawa, T.1    Kita, Y.2    Timasheff, S.N.3
  • 25
    • 84869195336 scopus 로고    scopus 로고
    • Denaturation and Preservation of Globular Proteins: The Role of DMSO
    • Giugliarelli, A.; Paolantoni, M.; Morresi, A.; Sassi, P. Denaturation and Preservation of Globular Proteins: the Role of DMSO J. Phys. Chem. B 2012, 116, 13361-13367
    • (2012) J. Phys. Chem. B , vol.116 , pp. 13361-13367
    • Giugliarelli, A.1    Paolantoni, M.2    Morresi, A.3    Sassi, P.4
  • 26
    • 0034005357 scopus 로고    scopus 로고
    • Amyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution
    • Goda, S.; Takano, K.; Yamagata, Y.; Nagata, R.; Akutsu, H.; Maki, S.; Namba, K.; Yutani, K. Amyloid Protofilament Formation of Hen Egg Lysozyme in Highly Concentrated Ethanol Solution Protein Sci. 2000, 9, 369-375 (Pubitemid 30127010)
    • (2000) Protein Science , vol.9 , Issue.2 , pp. 369-375
    • Goda, S.1    Takano, K.2    Yamagata, Y.3    Nagata, R.4    Akutsu, H.5    Maki, S.6    Namba, K.7    Yutani, K.8
  • 27
    • 0344198173 scopus 로고    scopus 로고
    • Temperature-Induced Dissociation of Protein Aggregates: Accessing the Denatured State
    • DOI 10.1021/bi035623e
    • Meersman, F.; Heremans, K. Temperature-Induced Dissociation of Protein Aggregates: Accessing the Denatured State Biochemistry 2003, 42, 14234-14241 (Pubitemid 37499420)
    • (2003) Biochemistry , vol.42 , Issue.48 , pp. 14234-14241
    • Meersman, F.1    Heremans, K.2
  • 28
    • 67349094537 scopus 로고    scopus 로고
    • Infrared Techniques for Quantifying Protein Structural Stability
    • Vrettos, J. S.; Meuse, C. W. Infrared Techniques for Quantifying Protein Structural Stability Anal. Biochem. 2009, 390, 14-20
    • (2009) Anal. Biochem. , vol.390 , pp. 14-20
    • Vrettos, J.S.1    Meuse, C.W.2
  • 29
    • 0026332511 scopus 로고
    • Comparison of Alpha.-Lactalbumin ond Lysozyme Using Vibrational Circular Dichroism. Evidence for a Difference in Crystal and Solution Structures
    • Urbanova, M.; Dukor, R. K.; Pancoska, P.; Gupta, V. P.; Keiderling, T. A. Comparison of Alpha.-Lactalbumin ond Lysozyme Using Vibrational Circular Dichroism. Evidence for a Difference in Crystal and Solution Structures Biochemistry 1991, 30, 10479-10485
    • (1991) Biochemistry , vol.30 , pp. 10479-10485
    • Urbanova, M.1    Dukor, R.K.2    Pancoska, P.3    Gupta, V.P.4    Keiderling, T.A.5
  • 30
    • 0021474457 scopus 로고
    • Vibrational Circular Dichroism of Polypeptides. III. Film Studies of Several α-Helical and β-Sheet Polypeptides
    • Sen, A. C.; Keiderling, T. A. Vibrational Circular Dichroism of Polypeptides. III. Film Studies of Several α-Helical and β-Sheet Polypeptides Biopolymers 1984, 23, 1533-1545
    • (1984) Biopolymers , vol.23 , pp. 1533-1545
    • Sen, A.C.1    Keiderling, T.A.2
  • 31
    • 0035814332 scopus 로고    scopus 로고
    • Differentiation of β-sheet-forming structures: Ab initio-based simulations of IR absorption and vibrational CD for model peptide and protein β-sheets
    • DOI 10.1021/ja0116627
    • Kubelka, J.; Keiderling, T. A. Differentiation of β-Sheet-Forming Structures: Ab Initio-Based Simulations of IR Absorption and Vibrational CD for Model Peptide and Protein β-Sheets J. Am. Chem. Soc. 2001, 123, 12048-12058 (Pubitemid 33135036)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.48 , pp. 12048-12058
    • Kubelka, J.1    Keiderling, T.A.2
  • 32
    • 0038546798 scopus 로고    scopus 로고
    • Optical spectroscopic investigations of model β-sheet hairpins in aqueous solution
    • DOI 10.1021/ja030039e
    • Hilario, J.; Kubelka, J.; Keiderling, T. A. Optical Spectroscopic Investigations of Model β-Sheet Hairpins in Aqueous Solution J. Am. Chem. Soc. 2003, 125, 7562-7574 (Pubitemid 36750277)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.25 , pp. 7562-7574
    • Hilario, J.1    Kubelka, J.2    Keiderling, T.A.3
  • 33
    • 0001314765 scopus 로고
    • Vibrational Circular Dichroism of Polypeptides. 8. Poly(Lysine) Conformations as a Function of pH in Aqueous Solution
    • Yasui, S. C.; Keiderling, T. A. Vibrational Circular Dichroism of Polypeptides. 8. Poly(Lysine) Conformations as a Function of pH in Aqueous Solution J. Am. Chem. Soc. 1986, 108, 5576-5581
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 5576-5581
    • Yasui, S.C.1    Keiderling, T.A.2
  • 34
    • 0022588380 scopus 로고
    • Vibrational Circular Dichroism of Polypeptides. VI. Polytyrosine α-Helical and Random-Coil Results
    • Yasui, S. C.; Keiderling, T. A. Vibrational Circular Dichroism of Polypeptides. VI. Polytyrosine α-Helical and Random-Coil Results Biopolymers 1986, 25, 5-15
    • (1986) Biopolymers , vol.25 , pp. 5-15
    • Yasui, S.C.1    Keiderling, T.A.2
  • 36
    • 18444365588 scopus 로고    scopus 로고
    • Solvent effects on IR and VCD spectra of helical peptides: DFT-based static spectral simulations with explicit water
    • DOI 10.1021/jp0506078
    • Kubelka, J.; Huang, R.; Keiderling, T. A. Solvent Effects on IR and VCD Spectra of Helical Peptides: DFT-Based Static Spectral Simulations with Explicit Water J. Phys. Chem. B 2005, 109, 8231-8243 (Pubitemid 40644050)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.16 , pp. 8231-8243
    • Kubelka, J.1    Huang, R.2    Keiderling, T.A.3
  • 37
    • 0022067726 scopus 로고
    • Vibrational Circular Dichroism in Amino Acids and Peptides. 10. Fourier Transform VCD and Fourier Self-Deconvolution of the Amide i Region of Poly(γ-Benzyl-L-Glutamate)
    • Lipp, E. D.; Nafie, L. A. Vibrational Circular Dichroism in Amino Acids and Peptides. 10. Fourier Transform VCD and Fourier Self-Deconvolution of the Amide I Region of Poly(γ-Benzyl-L-Glutamate) Biopolymers 1985, 24, 799-812
    • (1985) Biopolymers , vol.24 , pp. 799-812
    • Lipp, E.D.1    Nafie, L.A.2
  • 39
    • 11244340520 scopus 로고    scopus 로고
    • Thermally induced fibrillar aggregation of hen egg white lysozyme
    • DOI 10.1529/biophysj.104.048819
    • Arnaudov, L. N.; de Vries, R. Thermally Induced Fibrillar Aggregation of Hen Egg White Lysozyme Biophys. J. 2005, 88, 515-526 (Pubitemid 40070697)
    • (2005) Biophysical Journal , vol.88 , Issue.1 , pp. 515-526
    • Arnaudov, L.N.1    De Vries, R.2
  • 40
    • 0031744109 scopus 로고    scopus 로고
    • Influence of pH on lysozyme conformation revealed by dielectric spectroscopy
    • DOI 10.1016/S0927-7765(98)00048-4, PII S0927776598000484
    • Bonincontro, A.; De Francesco, A.; Onori, G. Influence of pH on Lysozyme Conformation Revealed by Dielectric Spectroscopy Colloids Surf., B 1998, 12, 1-5 (Pubitemid 28561563)
    • (1998) Colloids and Surfaces B: Biointerfaces , vol.12 , Issue.1 , pp. 1-5
    • Bonincontro, A.1    De Francesco, A.2    Onori, G.3
  • 41
    • 34547232128 scopus 로고    scopus 로고
    • Gelation of a model globular protein
    • DOI 10.1002/masy.200750515
    • Yan, H.; Saiani, A.; Miller, A. F. Gelation of a Model Globular Protein Macromol. Symp. 2007, 251, 112-117 (Pubitemid 47118985)
    • (2007) Macromolecular Symposia , vol.251 , pp. 112-117
    • Yan, H.1    Saiani, A.2    Miller, A.F.3
  • 43
    • 4644336155 scopus 로고    scopus 로고
    • Rheological Study of Lysozyme in Dimethyl Sulfoxide + Water Solution at 298.15 K
    • Kamiyama, T.; Morita, M.; Kimura, T. Rheological Study of Lysozyme in Dimethyl Sulfoxide + Water Solution at 298.15 K J. Chem. Eng. Data 2004, 49, 1350-1353
    • (2004) J. Chem. Eng. Data , vol.49 , pp. 1350-1353
    • Kamiyama, T.1    Morita, M.2    Kimura, T.3
  • 44
    • 77956812220 scopus 로고    scopus 로고
    • Direct Observation and pH Control of Reversed Supramolecular Chirality in Insulin Fibrils by Vibrational Circular Dichroism
    • Kurouski, D.; Lombardi, R. A.; Dukor, R. K.; Lednev, I. K.; Nafie, L. A. Direct Observation and pH Control of Reversed Supramolecular Chirality in Insulin Fibrils by Vibrational Circular Dichroism Chem. Commun. 2010, 46, 7154-7156
    • (2010) Chem. Commun. , vol.46 , pp. 7154-7156
    • Kurouski, D.1    Lombardi, R.A.2    Dukor, R.K.3    Lednev, I.K.4    Nafie, L.A.5
  • 45
  • 47
    • 0034716942 scopus 로고    scopus 로고
    • Direct Visualisation of the β-sheet Structure of Synthetic Alzheimer's Amyloid
    • Serpell, L. C.; Smith, J. M. Direct Visualisation of the β-sheet Structure of Synthetic Alzheimer's Amyloid J. Mol. Biol. 2000, 299, 225-231
    • (2000) J. Mol. Biol. , vol.299 , pp. 225-231
    • Serpell, L.C.1    Smith, J.M.2
  • 48
    • 80052823373 scopus 로고    scopus 로고
    • Spiral Superstructures of Amyloid-Like Fibrils of Polyglutamic Acid: An Infrared Absorption and Vibrational Circular Dichroism Study
    • Fulara, A.; Lakhani, A.; Wójcik, S.; Nieznańska, H.; Keiderling, T. A.; Dzwolak, W. Spiral Superstructures of Amyloid-Like Fibrils of Polyglutamic Acid: An Infrared Absorption and Vibrational Circular Dichroism Study J. Phys. Chem. B 2011, 115, 11010-11016
    • (2011) J. Phys. Chem. B , vol.115 , pp. 11010-11016
    • Fulara, A.1    Lakhani, A.2    Wójcik, S.3    Nieznańska, H.4    Keiderling, T.A.5    Dzwolak, W.6


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