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Volumn 5790, Issue , 2005, Pages 54-65

THz characterization of lysozyme at different conformations

Author keywords

Denaturation; Frozen; Liquid; Protein lysozyme; Resonance modes; THz Spectroscopy

Indexed keywords

CONFORMATIONS; ENZYMES; IMAGING SYSTEMS; LIGHT TRANSMISSION; LIQUIDS; NATURAL FREQUENCIES; PRECIPITATION (CHEMICAL); RESONANCE;

EID: 26844502135     PISSN: 0277786X     EISSN: None     Source Type: Conference Proceeding    
DOI: 10.1117/12.603581     Document Type: Conference Paper
Times cited : (5)

References (36)
  • 2
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide i infrared spectra
    • Aichun Dong, Ping Huang, and Winslow S. Caughey, "Protein Secondary Structures in Water from Second-Derivative Amide I Infrared Spectra", Biochemistry 1990, 29, 3303-3308].
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 3
    • 0031575421 scopus 로고    scopus 로고
    • Accelaration of the folding of Hen Lysozyme by Trifluoroethanol
    • H. Lu, M. Buck, S. Radford and C. Dobson, "Accelaration of the folding of Hen Lysozyme by Trifluoroethanol, J. Mol. Biol. 1997, 265, 112-117.
    • (1997) J. Mol. Biol. , vol.265 , pp. 112-117
    • Lu, H.1    Buck, M.2    Radford, S.3    Dobson, C.4
  • 4
    • 0034736271 scopus 로고    scopus 로고
    • Organic cosolvents and hen egg white lysozyme folding
    • B. Lai, A. Cao, L. Lai, "Organic cosolvents and hen egg white lysozyme folding", Biochimica et Biophysica Acta 1543 (2000) 115-122.
    • (2000) Biochimica et Biophysica Acta , vol.1543 , pp. 115-122
    • Lai, B.1    Cao, A.2    Lai, L.3
  • 5
    • 0344198173 scopus 로고    scopus 로고
    • Temperature-induced dissociation of protein aggregates: Accessing the denatured state
    • F. Meersman, K. Heremans, "Temperature-Induced Dissociation of Protein Aggregates: Accessing the denatured State", Biochemistry 2003, 42, 14234-14241.
    • (2003) Biochemistry , vol.42 , pp. 14234-14241
    • Meersman, F.1    Heremans, K.2
  • 6
    • 0037196421 scopus 로고    scopus 로고
    • The unfolding mechanism and the disulfide structures of denatured lysozyme
    • J-Y. Chang, L. Li "The unfolding mechanism and the disulfide structures of denatured lysozyme", FEBS Letters (Feder, of European Biochemical Soc.) 511 (2002) 73-78.
    • (2002) FEBS Letters (Feder, of European Biochemical Soc.) , vol.511 , pp. 73-78
    • Chang, J.-Y.1    Li, L.2
  • 7
    • 0036892357 scopus 로고    scopus 로고
    • Equilibrium and kinetic folding of hen egg-white lysozyme under acidic conditions
    • K. Sasahara, M. Demura, K. Nitta, "Equilibrium and kinetic folding of hen egg-white lysozyme under acidic conditions", Proteins: structure, Functions, and Genetics, V49, 4, p.472-482, 2002.
    • (2002) Proteins: Structure, Functions, and Genetics , vol.49 , Issue.4 , pp. 472-482
    • Sasahara, K.1    Demura, M.2    Nitta, K.3
  • 8
    • 0033573999 scopus 로고    scopus 로고
    • Structure, thermostability, and conformational flexibility of hen egg-white lysozyme dissolved in glycerol
    • Biochemistry
    • T. Knubovets, J. Osterhout, P. Connoly, A. Klebanov, Structure, thermostability, and conformational flexibility of hen egg-white lysozyme dissolved in glycerol", Proc. Natl. Acad. Sci, USA, 96, 1262-1267, 1999, Biochemistry.
    • (1999) Proc. Natl. Acad. Sci, USA , vol.96 , pp. 1262-1267
    • Knubovets, T.1    Osterhout, J.2    Connoly, P.3    Klebanov, A.4
  • 9
    • 0030054978 scopus 로고    scopus 로고
    • Refolding of denaturated/reduced lysozyme at high concentration
    • B. Raman, T. Ramakrishna, Ch. Mohan Rao, "Refolding of Denaturated/Reduced Lysozyme at High Concentration", JBC, V.271, Nu29, pp 17067-17072, 1996.
    • (1996) JBC , vol.271 , Issue.29 , pp. 17067-17072
    • Raman, B.1    Ramakrishna, T.2    Mohan Rao, Ch.3
  • 10
    • 26844504754 scopus 로고    scopus 로고
    • A. Jabs, http://www.imb-jena.de/ImgLibDoc/ftir/IMAGE_FTIR.html.
    • Jabs, A.1
  • 11
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Jan6
    • Provencher SW, Glockner J. Estimation of globular protein secondary structure from circular dichroism. Biochemistry, 1981 Jan6;20(1):33-37
    • (1981) Biochemistry , vol.20 , Issue.1 , pp. 33-37
    • Provencher, S.W.1    Glockner, J.2
  • 12
    • 0019871893 scopus 로고
    • Information content in the curcular dichroism of proteins
    • Mar3
    • Hennessey JP Jr,johnson WC Jr. Information content in the curcular dichroism of proteins.Biochemistry 1981 Mar3;20(5):1085-94
    • (1981) Biochemistry , vol.20 , Issue.5 , pp. 1085-1094
    • Hennessey Jr., J.P.1    Johnson Jr., W.C.2
  • 13
    • 1942424127 scopus 로고    scopus 로고
    • Secondary-structure analysis of proteins by vacuum-ultraviolet circular dichroism spectroscopy
    • K. Matsuo, K. Yonehara, K. Gekko, "Secondary-Structure Analysis of Proteins by Vacuum-Ultraviolet Circular Dichroism Spectroscopy", J. Biochem. 135, 405-411 (2004).
    • (2004) J. Biochem. , vol.135 , pp. 405-411
    • Matsuo, K.1    Yonehara, K.2    Gekko, K.3
  • 14
    • 0032551666 scopus 로고    scopus 로고
    • Probing residue-level unfolding during lysozyme precipitation
    • S. T. Chang, E.J. Fernandez, "Probing Residue-Level Unfolding During Lysozyme Precipitation", Biotechnology and Bioengineering, 59, 144-155 (1998).
    • (1998) Biotechnology and Bioengineering , vol.59 , pp. 144-155
    • Chang, S.T.1    Fernandez, E.J.2
  • 15
    • 26844480185 scopus 로고
    • Structure & Functions, Eds. R. H. Sarma and M. H. Sarma (Adenine Press) and references therein
    • L. L. Van Zandt and V. K. Saxena, in Structure & Functions, Volume 1: Nucleic Acids, Eds. R. H. Sarma and M. H. Sarma (Adenine Press, 1992) and references therein.
    • (1992) Nucleic Acids , vol.1
    • Van Zandt, L.L.1    Saxena, V.K.2
  • 16
    • 84985726392 scopus 로고
    • Acoustic modes and nonbonded interactions of the double helix
    • W. N. Mei, M. Kohli, E. W. Prohofsky, and L. L. Van Zandt, "Acoustic Modes and Nonbonded Interactions of the Double Helix", Biopolymers, 20, 833-864 (1981)
    • (1981) Biopolymers , vol.20 , pp. 833-864
    • Mei, W.N.1    Kohli, M.2    Prohofsky, E.W.3    Van Zandt, L.L.4
  • 17
    • 0001653348 scopus 로고
    • Calculation of far-infrared absorption in polymer DNA
    • L. Young, V. V. Prabhu and E. W. Prohovsky, "Calculation of far-infrared absorption in polymer DNA", Phys. Rev. A 39, 3173 (1989).
    • (1989) Phys. Rev. A , vol.39 , pp. 3173
    • Young, L.1    Prabhu, V.V.2    Prohovsky, E.W.3
  • 18
    • 0025321519 scopus 로고
    • Vibrational fluctuations of hydrogen bonds in a DNA double helix with nonuniform base pairs
    • Y. Feng and E. M. Prohofski, "Vibrational fluctuations of hydrogen bonds in a DNA double helix with nonuniform base pairs", Biophys. J. 57, 547-553 (1990).
    • (1990) Biophys. J. , vol.57 , pp. 547-553
    • Feng, Y.1    Prohofski, E.M.2
  • 19
    • 0000933223 scopus 로고    scopus 로고
    • Normal mode analysis of a double-stranded DNA dodecamer d(CGCGAATTCGCG)
    • D. Lin, A. Matsumoto, and N. Go. "Normal mode analysis of a double-stranded DNA dodecamer d(CGCGAATTCGCG)", J.Chem. Phys. 107(9), 3684-3690 (1997).
    • (1997) J.Chem. Phys. , vol.107 , Issue.9 , pp. 3684-3690
    • Lin, D.1    Matsumoto, A.2    Go, N.3
  • 20
    • 0000213488 scopus 로고    scopus 로고
    • Calculation and analysis of low frequency normal modes for DNA
    • T. H. Duong and K. Zakrzewska. "Calculation and analysis of low frequency normal modes for DNA", J.Comp. Chem. 18(6), 796-811 (1997).
    • (1997) J.Comp. Chem. , vol.18 , Issue.6 , pp. 796-811
    • Duong, T.H.1    Zakrzewska, K.2
  • 23
    • 0035766112 scopus 로고    scopus 로고
    • Far-infrared phonon modes of selected RNA molecules
    • Instrumentation for Air Pollution and Global Atmospheric Monitoring, J.O.Jensen and R.L. Spellicy, ed.
    • T. Globus, M. Bykhovskaia, B. Gelmont, D.L.Woolard, "Far-infrared phonon modes of selected RNA molecules", Instrumentation for Air Pollution and Global Atmospheric Monitoring, J.O.Jensen and R.L. Spellicy, ed. Proceedings of SPIE Vol. 4574, 119-128 (2002).
    • (2002) Proceedings of SPIE , vol.4574 , pp. 119-128
    • Globus, T.1    Bykhovskaia, M.2    Gelmont, B.3    Woolard, D.L.4
  • 29
    • 2142769879 scopus 로고    scopus 로고
    • Terahertz Fourier transform characterization of biological materials in solid and liquid phases
    • Chemical and Biological Standoff Detection in the Terahertz Region, Providence, RI, Oct 2003
    • T. Globus, T. Khromova, D. Woolard and B. Gelmont, "Terahertz Fourier transform characterization of biological materials in solid and liquid phases", Chemical and Biological Standoff Detection in the Terahertz Region, Providence, RI, Oct 2003, Proceedings of SPIE Vol. 5268-2, pp. 10-18 (2004).
    • (2004) Proceedings of SPIE , vol.5268 , Issue.2 , pp. 10-18
    • Globus, T.1    Khromova, T.2    Woolard, D.3    Gelmont, B.4
  • 32
    • 1642431820 scopus 로고    scopus 로고
    • Continuous-wave terahertz Spectroscopy of biotin: Vibrational anharmonicity in the far-infrared
    • 2 February
    • T. M. Korter and D. F. Plusquellic, Continuous-wave terahertz Spectroscopy of biotin: vibrational anharmonicity in the far-infrared, Chemical Physics Letters, Volume 385, Issues 1-2, Pages 45-51 (2 February 2004).
    • (2004) Chemical Physics Letters , vol.385 , Issue.1-2 , pp. 45-51
    • Korter, T.M.1    Plusquellic, D.F.2
  • 34
    • 0031402313 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins and peptides in lipid bilayers
    • Cambridge University Press
    • Lukas K. Tamm and Suren A. Tatulian, "Infrared Spectroscopy of proteins and peptides in lipid bilayers", Quarterly Reviews of Biophysics 30, 4, pp365-429,1997, Cambridge University Press.
    • (1997) Quarterly Reviews of Biophysics , vol.30 , Issue.4 , pp. 365-429
    • Tamm, L.K.1    Tatulian, S.A.2
  • 35
  • 36
    • 0031575421 scopus 로고    scopus 로고
    • Accelaration of the folding of hen lysozyme by Trifluoroethanol
    • H. Lu, M. Buck, S. E.Radford, C. M. Dobson, "Accelaration of the folding of hen lysozyme by Trifluoroethanol", JMB (1997), 265, 112-117.
    • (1997) JMB , vol.265 , pp. 112-117
    • Lu, H.1    Buck, M.2    Radford, S.E.3    Dobson, C.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.