메뉴 건너뛰기




Volumn 14, Issue 2, 2005, Pages 368-374

Spectral magnitude effects on the analyses of secondary structure from circular dichroism spectroscopic data

Author keywords

Calibration; Circular dichroism (CD) spectroscopy; Secondary structure analyses; Synchrotron radiation circular dichroism (SRCD)

Indexed keywords

AVIDIN; CERULOPLASMIN; PROTEIN;

EID: 13244255213     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.041019905     Document Type: Article
Times cited : (54)

References (33)
  • 1
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised learning neural network
    • Andrade, M.A., Chacón, P., Merelo, J.J., and Morán, F. 1993. Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised learning neural network. Protein Eng. 6: 383-390.
    • (1993) Protein Eng. , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacón, P.2    Merelo, J.J.3    Morán, F.4
  • 2
    • 0022474744 scopus 로고
    • Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication
    • Compton, L.A. and Johnson Jr., W.C. 1986. Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal. Biochem. 155: 155-167.
    • (1986) Anal. Biochem. , vol.155 , pp. 155-167
    • Compton, L.A.1    Johnson Jr., W.C.2
  • 3
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. and Sander, C. 1983. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 4
    • 0033562619 scopus 로고    scopus 로고
    • Assigning secondary structure from protein coordinate data
    • King, S.M. and Johnson Jr., W.C. 1999. Assigning secondary structure from protein coordinate data. Proteins 35: 313-320.
    • (1999) Proteins , vol.35 , pp. 313-320
    • King, S.M.1    Johnson Jr., W.C.2
  • 5
    • 0036965576 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism and conventional circular dichroism spectroscopy: A comparison
    • Lees, J. and Wallace, B.A. 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.1    Wallace, B.A.2
  • 6
    • 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
  • 7
    • 0027062886 scopus 로고
    • Control of phosphorylase-b conformation by a modified cofactor-Crystallographic studies on R-state glycogen-phosphorylase reconstituted with pyridoxal 5′-diphosphate
    • Leonidas, D.D., Oikonomakos, N.G., Papageorgiou, A.C., Acharya, K.R., Barford, D., and Johnson, L.N. 1992. Control of phosphorylase-b conformation by a modified cofactor-Crystallographic studies on R-state glycogen-phosphorylase reconstituted with pyridoxal 5′-diphosphate. Protein Sci. 1: 1112-1122.
    • (1992) Protein Sci. , vol.1 , pp. 1112-1122
    • Leonidas, D.D.1    Oikonomakos, N.G.2    Papageorgiou, A.C.3    Acharya, K.R.4    Barford, D.5    Johnson, L.N.6
  • 8
    • 0036168995 scopus 로고    scopus 로고
    • DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra
    • Lobley, A., Whitmore, L., and Wallace, B.A. 2002. DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 18: 211-212.
    • (2002) Bioinformatics , vol.18 , pp. 211-212
    • Lobley, A.1    Whitmore, L.2    Wallace, B.A.3
  • 10
    • 0023656828 scopus 로고
    • Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra
    • Manavalan, P. and Johnson Jr., W.C. 1987. Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal. Biochem. 167: 76-85.
    • (1987) Anal. Biochem. , vol.167 , pp. 76-85
    • Manavalan, P.1    Johnson Jr., W.C.2
  • 13
    • 0035368579 scopus 로고    scopus 로고
    • Circular dichroism studies on proteins in films and in solution: Estimation of secondary structure by g-factor analysis
    • McPhie, P. 2001. Circular dichroism studies on proteins in films and in solution: Estimation of secondary structure by g-factor analysis. Anal. Biochem. 293: 109-119.
    • (2001) Anal. Biochem. , vol.293 , pp. 109-119
    • McPhie, P.1
  • 14
    • 0348147599 scopus 로고    scopus 로고
    • Calibration and standardisation of synchrotron radiation circular dichroism and conventional circular dichroism (cCD) spectrophotometers
    • Miles, A.J., Wien, F., Lees, J.G., Rodger, A., Janes, R.W., and Wallace, B.A. 2003. Calibration and standardisation of synchrotron radiation circular dichroism and conventional circular dichroism (cCD) spectrophotometers. Spectroscopy 17: 653-661.
    • (2003) Spectroscopy , vol.17 , pp. 653-661
    • Miles, A.J.1    Wien, F.2    Lees, J.G.3    Rodger, A.4    Janes, R.W.5    Wallace, B.A.6
  • 15
    • 8844221903 scopus 로고    scopus 로고
    • Redetermination of the extinction coefficient of camphor-10-sulfonic acid, a calibration standard for circular dichroism spectroscopy
    • Miles, A.J., Wien, F., and Wallace, B.A. 2004. Redetermination of the extinction coefficient of camphor-10-sulfonic acid, a calibration standard for circular dichroism spectroscopy. Anal. Biochem. 335: 338-339.
    • (2004) Anal. Biochem. , vol.335 , pp. 338-339
    • Miles, A.J.1    Wien, F.2    Wallace, B.A.3
  • 16
    • 12844253803 scopus 로고    scopus 로고
    • Calibration and standardisation of synchrotron radiation and conventional circular dichroism spectrometers. Part 2: Factors affecting magnitude and wavelength
    • in press
    • 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 (in press).
    • (2005) Spectroscopy
    • Miles, A.J.1    Wien, F.2    Lees, J.G.3    Wallace, B.A.4
  • 19
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher, S.W. and Glockner, J. 1981. Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20: 33-37.
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glockner, J.2
  • 20
    • 0037677275 scopus 로고    scopus 로고
    • Protein concentration is not an absolute prerequisite for the determination of secondary structure from circular dichroism spectra: A new scaling method
    • Raussens, V., Ruysschaert, J.-M., and Goormaghtigh, E. 2003. Protein concentration is not an absolute prerequisite for the determination of secondary structure from circular dichroism spectra: A new scaling method. Anal. Biochem. 319: 114-121.
    • (2003) Anal. Biochem. , vol.319 , pp. 114-121
    • Raussens, V.1    Ruysschaert, J.-M.2    Goormaghtigh, E.3
  • 21
    • 0042553279 scopus 로고
    • Smoothing and differentiation of data by simplified least squares procedures
    • Savitsky, A. and Golay, M.J.E. 1964. Smoothing and differentiation of data by simplified least squares procedures. Anal. Chem. 36: 1627-1639.
    • (1964) Anal. Chem. , vol.36 , pp. 1627-1639
    • Savitsky, A.1    Golay, M.J.E.2
  • 23
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from CD spectra: Comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set
    • Sreerama, N. and Woody, R.W. 2000. Estimation of protein secondary structure from CD spectra: Comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set. Anal. Biochem. 282: 252-260.
    • (2000) Anal. Biochem. , vol.282 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 24
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of helical and strand segments in proteins using CD spectroscopy
    • Sreerama, N., Venyaminov, S.Y., and Woody, R.W. 1999. Estimation of the number of helical and strand segments in proteins using CD spectroscopy. Protein Sci. 8: 370-380.
    • (1999) Protein Sci. , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 25
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from CD spectra: Inclusion of denatured proteins with native protein in the analysis
    • -. 2000. Estimation of protein secondary structure from CD spectra: Inclusion of denatured proteins with native protein in the analysis. Anal. Biochem. 287: 243-251.
    • (2000) Anal. Biochem. , vol.287 , pp. 243-251
  • 26
    • 0033062612 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin at 2.5 Å resolution
    • Sugio, S., Kashima, A., Mochizuki, S., Noda, M., and Kobayashi, K. 1999. Crystal structure of human serum albumin at 2.5 Å resolution. Protein Eng. 12: 439-446.
    • (1999) Protein Eng. , vol.12 , pp. 439-446
    • Sugio, S.1    Kashima, A.2    Mochizuki, S.3    Noda, M.4    Kobayashi, K.5
  • 28
    • 0034345294 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism spectroscopy as a tool for investigating protein structures
    • Wallace, B.A. 2000. Synchrotron radiation circular dichroism spectroscopy as a tool for investigating protein structures. J. Synch. Rad. 7: 289-295.
    • (2000) J. Synch. Rad. , vol.7 , pp. 289-295
    • Wallace, B.A.1
  • 29
    • 0023652252 scopus 로고
    • Differential absorption flattening optical effects are significant in the circular dichroism spectra of large membrane fragments
    • Wallace, B.A. and Teeters, C.L. 1987. Differential absorption flattening optical effects are significant in the circular dichroism spectra of large membrane fragments. Biochemistry 26: 65-70.
    • (1987) Biochemistry , vol.26 , pp. 65-70
    • Wallace, B.A.1    Teeters, C.L.2
  • 30
    • 13244293443 scopus 로고    scopus 로고
    • Biomedical applications of synchrotron radiation circular dichroism spectroscopy: Identification of mutant proteins associated with disease and development of a reference database for fold motifs
    • Wallace, B.A., Wien, F., Miles, A.J., Lees, J.G., Huffman, S.V., Evans, P., Wistow, G.J., and Slingsby, C. 2004. Biomedical applications of synchrotron radiation circular dichroism spectroscopy: Identification of mutant proteins associated with disease and development of a reference database for fold motifs. Faraday Discuss. 17: 653-661.
    • (2004) Faraday Discuss , vol.17 , pp. 653-661
    • Wallace, B.A.1    Wien, F.2    Miles, A.J.3    Lees, J.G.4    Huffman, S.V.5    Evans, P.6    Wistow, G.J.7    Slingsby, C.8
  • 31
    • 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-W673.
    • (2004) Nucleic Acids Res. , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 33
    • 3042958993 scopus 로고    scopus 로고
    • The X-ray structure of human serum ceruloplasmin at 3.1 angstrom: Nature of the copper centres
    • Zaitseva, I., Zaitsev, V., Card, G., Moshkov, K., Bax, B., Ralph, A., and Lindley, P. 1996. The X-ray structure of human serum ceruloplasmin at 3.1 angstrom: Nature of the copper centres. J. Biol. Inorg. Chem. 1: 15-23.
    • (1996) J. Biol. Inorg. Chem. , vol.1 , pp. 15-23
    • Zaitseva, I.1    Zaitsev, V.2    Card, G.3    Moshkov, K.4    Bax, B.5    Ralph, A.6    Lindley, P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.