메뉴 건너뛰기




Volumn 752, Issue , 2011, Pages 59-72

Circular Dichroism and Its Use in Protein-Folding Studies

Author keywords

Circular dichroism; Protein folding; Protein secondary and tertiary structure; Stopped flow; Ultraviolet spectroscopy

Indexed keywords

PROTEIN;

EID: 79960991394     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1007/978-1-60327-223-0_5     Document Type: Chapter
Times cited : (8)

References (23)
  • 2
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K.A., and Chen, H.S. (1997) From Levinthal to pathways to funnels. Nature Struct. Biol. 4, 10–19.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chen, H.S.2
  • 6
    • 0003786121 scopus 로고    scopus 로고
    • Aromatic and cystine side-chain circular dichroism in proteins
    • Fasman, G.D., ed.), Plenum Press, New York and London
    • Woody, R.W., and Dunker, A.K. (1996) Aromatic and cystine side-chain circular dichroism in proteins, in Circular Dichroism and the Conformational Analysis of Biomolecules (Fasman, G.D., ed.), Plenum Press, New York and London, pp. 109–157.
    • (1996) Circular Dichroism and the Conformational Analysis of Biomolecules , pp. 109-157
    • Woody, R.W.1    Dunker, A.K.2
  • 7
    • 0001440712 scopus 로고    scopus 로고
    • Circular dichroism instrumentation
    • Fasman, G.D., ed.), Plenum Press, New York and London
    • Johnson, W.C., Jr. (1996) Circular dichroism instrumentation, in Circular Dichroism and the Conformational Analysis of Biomolecules (Fasman, G.D., ed.), Plenum Press, New York and London, pp. 635–652.
    • (1996) Circular Dichroism and the Conformational Analysis of Biomolecules , pp. 635-652
    • Johnson, W.C.1
  • 8
    • 3843085404 scopus 로고    scopus 로고
    • CD12: A new high-flux beamline for ultraviolet and vac-uum-ultraviolet circular dichroism on the SRS, Daresbury
    • Clarke, D.T., and Jones, G.R. (2004) CD12: a new high-flux beamline for ultraviolet and vac-uum-ultraviolet circular dichroism on the SRS, Daresbury. J. Synch. Rad. 11, 142–149.
    • (2004) J. Synch. Rad. , vol.11 , pp. 142-149
    • Clarke, D.T.1    Jones, G.R.2
  • 9
    • 39449096976 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism (SRCD) spectroscopy: New beamlines and new applications in biology
    • Miles, A.J., Hoffman, S.V., Tao, Y., Janes, R.W., and Wallace, B.A. (2007) Synchrotron radiation circular dichroism (SRCD) spectroscopy: New beamlines and new applications in biology, Spectroscopy 21, 245–255.
    • (2007) Spectroscopy , vol.21 , pp. 245-255
    • Miles, A.J.1    Hoffman, S.V.2    Tao, Y.3    Janes, R.W.4    Wallace, B.A.5
  • 10
    • 0004181611 scopus 로고    scopus 로고
    • Springer, Berlin, Heidelberg, New York
    • Nölting, B. (2005) in Protein Folding Kinetics, Springer, Berlin, Heidelberg, New York, pp. 98–104.
    • (2005) Protein Folding Kinetics , pp. 98-104
    • Nölting, B.1
  • 12
    • 0000986867 scopus 로고
    • Rapid mixing: Stopped flow
    • Gibson, Q.H. (1969) Rapid mixing: Stopped flow. Meth. Enzymol. 16, 187–228.
    • (1969) Meth. Enzymol. , vol.16 , pp. 187-228
    • Gibson, Q.H.1
  • 13
    • 0018882456 scopus 로고    scopus 로고
    • Recent Developments in the Stopped-Flow Method for the Study of Fast Reactions
    • Glick, D. ed.), Wiley, New York
    • Hiromi, K. (2006) Recent Developments in the Stopped-Flow Method for the Study of Fast Reactions. In Methods of Biochemical Analysis, Volume 26 (Glick, D. ed.), Wiley, New York, pp. 137–164.
    • (2006) Methods of Biochemical Analysis, Volume 26 , pp. 137-164
    • Hiromi, K.1
  • 14
    • 34548826481 scopus 로고    scopus 로고
    • Infared Temperature-Jump Study of the Folding Dynamics of a-Helices and b-Hairpins
    • Bai, Y., and Nussinov, R., eds.), Humana Press, New Jersey
    • Gai, F., Du, D., and Xu, Y. (2007) Infared Temperature-Jump Study of the Folding Dynamics of a-Helices and b-Hairpins. In Protein Folding Protocols (Bai, Y., and Nussinov, R., eds.), Humana Press, New Jersey, pp. 1–20.
    • (2007) Protein Folding Protocols , pp. 1-20
    • Gai, F.1    Du, D.2    Xu, Y.3
  • 15
    • 0002364711 scopus 로고    scopus 로고
    • Theory of Circular Dichroism of Proteins
    • Fasman, G.D., ed.), Plenum Press, New York and London
    • Woody, R.W. (1996) Theory of Circular Dichroism of Proteins, in Circular Dichroism and the Conformational Analysis of Biomolecules (Fasman, G.D., ed.), Plenum Press, New York and London, pp. 25–67.
    • (1996) Circular Dichroism and the Conformational Analysis of Biomolecules , pp. 25-67
    • Woody, R.W.1
  • 16
    • 1642264875 scopus 로고    scopus 로고
    • Applications of extended ultra-violet circular dichroism spectroscopy in biology and medicine
    • Jones, G.R., and Clarke, D.T. (2004) Applications of extended ultra-violet circular dichroism spectroscopy in biology and medicine. Faraday Discuss. 126, 223–236.
    • (2004) Faraday Discuss , vol.126 , pp. 223-236
    • Jones, G.R.1    Clarke, D.T.2
  • 17
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • Whitmore, L. and Wallace, B.A. (2008) Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 89, 392–400.
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 18
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore, L. and Wallace, B.A. (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32, W668-673.
    • (2004) Nucleic Acids Res , vol.32 , pp. W668-W673
    • Whitmore, L.1    Wallace, B.A.2
  • 21
    • 4644319196 scopus 로고    scopus 로고
    • CDtool-An Integrated Software Package for Circular Dichroism Spectroscopic Data Processing, Analysis and Archiving
    • Lees, J.G., Smith, B.R., Wien, F., Miles, A. J., and Wallace, B.A. (2004) CDtool-An Integrated Software Package for Circular Dichroism Spectroscopic Data Processing, Analysis and Archiving. Anal. Biochem. 332, 285–289.
    • (2004) Anal. Biochem. , vol.332 , pp. 285-289
    • Lees, J.G.1    Smith, B.R.2    Wien, F.3    Miles, A.J.4    Wallace, B.A.5
  • 22
    • 40649090353 scopus 로고    scopus 로고
    • Concentration-independent estimation of protein secondary structure by circular dichroism: A comparison of methods
    • McPhie, P. (2008) Concentration-independent estimation of protein secondary structure by circular dichroism: a comparison of methods. Anal. Biochem. 375, 379–381.
    • (2008) Anal. Biochem. , vol.375 , pp. 379-381
    • McPhie, P.1
  • 23
    • 12844253803 scopus 로고    scopus 로고
    • Calibration and standardisation of synchrotron radiation and conventional circular dichroism spectrometers. Part 2: Factors affecting magnitude and wavelength
    • Miles, A.J., Wien, F., Lees, J.G., and Wallace B.A. (2005) Calibration and standardisation of synchrotron radiation and conventional circular dichroism spectrometers. Part 2: factors affecting magnitude and wavelength. Spectroscopy 19, 43–51.
    • (2005) Spectroscopy , vol.19 , pp. 43-51
    • Miles, A.J.1    Wien, F.2    Lees, J.G.3    Wallace, B.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.