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Volumn 1751, Issue 2, 2005, Pages 119-139

How to study proteins by circular dichroism

Author keywords

Circular dichroism; Ligand binding; Protein folding; Protein structure; Secondary structure

Indexed keywords

ALPHA LACTALBUMIN; BUFFER; CELL EXTRACT; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; PEPTIDE; PROTEIN; SOLVENT;

EID: 23444456924     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.06.005     Document Type: Review
Times cited : (2647)

References (85)
  • 2
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • P. Nissen, N. Ban, J. Hansen, P.B. Moore, and T.A. Steitz The structural basis of ribosome activity in peptide bond synthesis Science 289 2000 920 930
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Ban, N.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 3
    • 33644574085 scopus 로고    scopus 로고
    • The FTIR/VCD spectroscopy as an informative tool for the investigation of large supramolecular complexes of biological macromolecules
    • (in press).
    • A. Polyanichko, H. Wieser, The FTIR/VCD spectroscopy as an informative tool for the investigation of large supramolecular complexes of biological macromolecules. Biopolymers (in press).
    • Biopolymers
    • Polyanichko, A.1    Wieser, H.2
  • 4
    • 4143109168 scopus 로고    scopus 로고
    • The multi-mode polarization modulation spectrometer: Part 1. Simultaneous detection of absorption, turbidity, and optical activity
    • T. Arvinte, T.T. Bui, A.A. Dahab, B. Demeule, A.F. Drake, D. Elhag, and P. King The multi-mode polarization modulation spectrometer: part 1. Simultaneous detection of absorption, turbidity, and optical activity Anal. Biochem. 332 2004 46 57
    • (2004) Anal. Biochem. , vol.332 , pp. 46-57
    • Arvinte, T.1    Bui, T.T.2    Dahab, A.A.3    Demeule, B.4    Drake, A.F.5    Elhag, D.6    King, P.7
  • 8
    • 0034584873 scopus 로고    scopus 로고
    • The use of circular dichroism in the investigation of protein structure and function
    • S.M. Kelly, and N.C. Price The use of circular dichroism in the investigation of protein structure and function Curr. Prot. Pept. Sci. 1 2000 349 384
    • (2000) Curr. Prot. Pept. Sci. , vol.1 , pp. 349-384
    • Kelly, S.M.1    Price, N.C.2
  • 10
    • 1642546383 scopus 로고    scopus 로고
    • Computation and analysis of protein circular dichroism spectra
    • N. Sreerama, and R.W. Woody Computation and analysis of protein circular dichroism spectra Methods Enzymol. 383 2004 318 351
    • (2004) Methods Enzymol. , vol.383 , pp. 318-351
    • Sreerama, N.1    Woody, R.W.2
  • 11
    • 0347994116 scopus 로고    scopus 로고
    • On the analysis of membrane protein circular dichroism spectra
    • N. Sreerama, and R.W. Woody On the analysis of membrane protein circular dichroism spectra Protein Sci. 13 2004 100 112
    • (2004) Protein Sci. , vol.13 , pp. 100-112
    • Sreerama, N.1    Woody, R.W.2
  • 12
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • N. Sreerama, and R.W. Woody A self-consistent method for the analysis of protein secondary structure from circular dichroism Anal. Biochem. 209 1993 32 44
    • (1993) Anal. Biochem. , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 13
    • 0023656828 scopus 로고
    • Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra
    • P. Manavalan, and W.C. Johnson Jr. Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra Anal. Biochem. 167 1987 76 85
    • (1987) Anal. Biochem. , vol.167 , pp. 76-85
    • Manavalan, P.1    Johnson Jr., W.C.2
  • 14
    • 0033562629 scopus 로고    scopus 로고
    • Analyzing protein circular dichroism spectra for accurate secondary structures
    • W.C. Johnson Analyzing protein circular dichroism spectra for accurate secondary structures Proteins: Struct. Funct. Genet. 35 1999 307 312
    • (1999) Proteins: Struct. Funct. Genet. , vol.35 , pp. 307-312
    • Johnson, W.C.1
  • 15
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised neural network
    • M.A. Andrade, P. Chacón, J.J. Merelo, and F. Morán Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised neural network Protein Eng. 6 1993 383 390
    • (1993) Protein Eng. , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacón, P.2    Merelo, J.J.3    Morán, F.4
  • 16
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • S.W. Provencher, and J. Glöckner Estimation of globular protein secondary structure from circular dichroism Biochemistry 20 1981 33 37
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glöckner, J.2
  • 17
    • 0036168995 scopus 로고    scopus 로고
    • DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra
    • A. Lobley, L. Whitmore, and B.A. Wallace DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra Bioinformatics 18 2002 211 212
    • (2002) Bioinformatics , vol.18 , pp. 211-212
    • Lobley, A.1    Whitmore, L.2    Wallace, B.A.3
  • 18
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, An online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • L. Whitmore, and B.A. Wallace DICHROWEB, An online server for protein secondary structure analyses from circular dichroism spectroscopic data Nucleic Acids Res. 32 2004 W668 W673
    • (2004) Nucleic Acids Res. , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 19
    • 0033562629 scopus 로고    scopus 로고
    • Analyzing protein circular dichroism spectra for accurate secondary structures
    • W.C. Johnson Jr. Analyzing protein circular dichroism spectra for accurate secondary structures Proteins: Struct. Funct. Genet. 35 1999 307 312
    • (1999) Proteins: Struct. Funct. Genet. , vol.35 , pp. 307-312
    • Johnson Jr., W.C.1
  • 20
    • 0034345294 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism spectroscopy as a tool for investigating protein structures
    • B.A. Wallace Synchrotron radiation circular dichroism spectroscopy as a tool for investigating protein structures J. Synchrotron. Radiat. 7 2000 289 295
    • (2000) J. Synchrotron. Radiat. , vol.7 , pp. 289-295
    • Wallace, B.A.1
  • 21
    • 0035478472 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism spectroscopy of proteins: Secondary structure, fold recognition and structural genomics
    • B.A. Wallace, and R.W. Janes Synchrotron radiation circular dichroism spectroscopy of proteins: secondary structure, fold recognition and structural genomics Curr. Opin. Chem. Biol. 5 2001 567 571
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 567-571
    • Wallace, B.A.1    Janes, R.W.2
  • 22
    • 0026682931 scopus 로고
    • Solution conformations and aggregational properties of synthetic amyloid beta-peptides of Alzheimer's disease. Analysis of circular dichroism spectra
    • C.J. Barrow, A. Yasuda, P.T. Kenny, and M.G. Zagorski Solution conformations and aggregational properties of synthetic amyloid beta-peptides of Alzheimer's disease. Analysis of circular dichroism spectra J. Mol. Biol. 225 1992 1075 1093
    • (1992) J. Mol. Biol. , vol.225 , pp. 1075-1093
    • Barrow, C.J.1    Yasuda, A.2    Kenny, P.T.3    Zagorski, M.G.4
  • 23
    • 0031282147 scopus 로고    scopus 로고
    • Correcting the circular dichroism spectra of peptides for contributions of absorbing side chains
    • C. Krittanai, and W.C. Johnson Jr. Correcting the circular dichroism spectra of peptides for contributions of absorbing side chains Anal. Biochem. 253 1997 57 64
    • (1997) Anal. Biochem. , vol.253 , pp. 57-64
    • Krittanai, C.1    Johnson Jr., W.C.2
  • 24
    • 0242696058 scopus 로고    scopus 로고
    • Individual tyrosine side-chain contributions to circular dichroism of ribonuclease
    • A.Y. Woody, and R.W. Woody Individual tyrosine side-chain contributions to circular dichroism of ribonuclease Biopolymers 72 2003 500 513
    • (2003) Biopolymers , vol.72 , pp. 500-513
    • Woody, A.Y.1    Woody, R.W.2
  • 25
    • 0027959547 scopus 로고
    • Assignment of the contribution of the tryptophan residues to the circular dichroism spectrum of human carbonic anhydrase II
    • P.-O. Freskgård, L.-G. Mårtensson, P. Jonasson, B.-H. Jonsson, and U. Carlsson Assignment of the contribution of the tryptophan residues to the circular dichroism spectrum of human carbonic anhydrase II Biochemistry 33 1994 14281 14288
    • (1994) Biochemistry , vol.33 , pp. 14281-14288
    • Freskgård, P.-O.1    Mårtensson, L.-G.2    Jonasson, P.3    Jonsson, B.-H.4    Carlsson, U.5
  • 26
    • 6344288893 scopus 로고    scopus 로고
    • Sensing of remote oxyanion binding at the DNA binding domain of the molybdate-dependent transcriptional regulator, ModE
    • D.H. Boxer, H. Zhang, D.G. Gourley, W.N. Hunter, S.M. Kelly, and N.C. Price Sensing of remote oxyanion binding at the DNA binding domain of the molybdate-dependent transcriptional regulator, ModE Org. Biomol. Chem. 2 2004 2829 2837
    • (2004) Org. Biomol. Chem. , vol.2 , pp. 2829-2837
    • Boxer, D.H.1    Zhang, H.2    Gourley, D.G.3    Hunter, W.N.4    Kelly, S.M.5    Price, N.C.6
  • 27
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • O.B. Ptitsyn Molten globule and protein folding Adv. Prot. Chem. 47 1995 83 229
    • (1995) Adv. Prot. Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 28
    • 12544252739 scopus 로고    scopus 로고
    • The key role of protein flexibility in modulating IgE interactions
    • N.E. Price, N.C. Price, S.M. Kelly, and J.M. McDonnell The key role of protein flexibility in modulating IgE interactions J. Biol. Chem. 280 2005 2324 2330
    • (2005) J. Biol. Chem. , vol.280 , pp. 2324-2330
    • Price, N.E.1    Price, N.C.2    Kelly, S.M.3    McDonnell, J.M.4
  • 30
    • 0029074117 scopus 로고
    • Active-site analysis of ferric P450 enzymes: Hydrogen-bonding effects on the circular dichroism spectra
    • L.A. Andersson, and J.A. Peterson Active-site analysis of ferric P450 enzymes: hydrogen-bonding effects on the circular dichroism spectra Biochem. Biophys. Res. Commun. 211 1995 389 395
    • (1995) Biochem. Biophys. Res. Commun. , vol.211 , pp. 389-395
    • Andersson, L.A.1    Peterson, J.A.2
  • 31
    • 5244255059 scopus 로고    scopus 로고
    • Calculations of spectroscopic properties of the LH2 bacteriochlorophyll- protein antenna complex from Rhodopseudomonas acidophila
    • R.G. Alden, E. Johnson, V. Nagarajan, W.W. Parson, C.J. Law, and R.J. Cogdell Calculations of spectroscopic properties of the LH2 bacteriochlorophyll- protein antenna complex from Rhodopseudomonas acidophila J. Phys. Chem. B101 1997 4667 4680
    • (1997) J. Phys. Chem. , vol.101 , pp. 4667-4680
    • Alden, R.G.1    Johnson, E.2    Nagarajan, V.3    Parson, W.W.4    Law, C.J.5    Cogdell, R.J.6
  • 32
    • 0025079267 scopus 로고
    • Unfolding-refolding of the domains in yeast phosphoglycerate kinase: Comparison with the isolated engineered domains
    • D. Missiakas, J.-M. Betton, P. Minard, and J.M. Yon Unfolding-refolding of the domains in yeast phosphoglycerate kinase: comparison with the isolated engineered domains Biochemistry 29 1990 8683 8689
    • (1990) Biochemistry , vol.29 , pp. 8683-8689
    • Missiakas, D.1    Betton, J.-M.2    Minard, P.3    Yon, J.M.4
  • 33
    • 0028205462 scopus 로고
    • Structural and enzymological analysis of the interaction of isolated domains of cytochrome P-450 BM3
    • A.W. Munro, J.G. Lindsay, J.R. Coggins, S.M. Kelly, and N.C. Price Structural and enzymological analysis of the interaction of isolated domains of cytochrome P-450 BM3 FEBS Lett. 343 1994 70 74
    • (1994) FEBS Lett. , vol.343 , pp. 70-74
    • Munro, A.W.1    Lindsay, J.G.2    Coggins, J.R.3    Kelly, S.M.4    Price, N.C.5
  • 34
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • C.N. Pace Determination and analysis of urea and guanidine hydrochloride denaturation curves Methods Enzymol. 131 1986 266 280
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 35
    • 0029061516 scopus 로고
    • Protein stability as a function of denaturant concentration: The thermal stability of barnase in the presence of urea
    • C.M. Johnson, and A.R. Fersht Protein stability as a function of denaturant concentration: the thermal stability of barnase in the presence of urea Biochemistry 34 1995 6795 6804
    • (1995) Biochemistry , vol.34 , pp. 6795-6804
    • Johnson, C.M.1    Fersht, A.R.2
  • 37
    • 0029964280 scopus 로고    scopus 로고
    • Cytotoxicity of prion protein peptide (PrP106-126) differs in mechanism from the cytotoxic activity of the Alzheimer's disease amyloid peptide, Aβ 25-35
    • J. Hope, M.S. Shearman, H.C. Baxter, A. Chong, S.M. Kelly, and N.C. Price Cytotoxicity of prion protein peptide (PrP106-126) differs in mechanism from the cytotoxic activity of the Alzheimer's disease amyloid peptide, Aβ 25-35 Neurodegeneration 5 1996 1 11
    • (1996) Neurodegeneration , vol.5 , pp. 1-11
    • Hope, J.1    Shearman, M.S.2    Baxter, H.C.3    Chong, A.4    Kelly, S.M.5    Price, N.C.6
  • 39
    • 0034383950 scopus 로고    scopus 로고
    • Protein folding: Progress made and promises ahead
    • S.E. Radford Protein folding: progress made and promises ahead Trends Biochem. Sci. 25 2000 611 618
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 611-618
    • Radford, S.E.1
  • 40
    • 2342655032 scopus 로고    scopus 로고
    • Demonstration of a low-energy on-pathway intermediate in a fast-folding protein by kinetics, protein engineering, and simulation
    • P. Jemth, S. Gianni, R. Day, B. Li, C.M. Johnson, V. Daggett, and A.R. Fersht Demonstration of a low-energy on-pathway intermediate in a fast-folding protein by kinetics, protein engineering, and simulation Proc. Natl. Acad. Sci. U. S. A. 101 2004 6450 6455
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 6450-6455
    • Jemth, P.1    Gianni, S.2    Day, R.3    Li, B.4    Johnson, C.M.5    Daggett, V.6    Fersht, A.R.7
  • 41
    • 3342991494 scopus 로고    scopus 로고
    • Experimental investigation of protein folding and misfolding
    • C.M. Dobson Experimental investigation of protein folding and misfolding Methods 34 2004 4 14
    • (2004) Methods , vol.34 , pp. 4-14
    • Dobson, C.M.1
  • 46
    • 0021736209 scopus 로고
    • Circular dichroism analyses of membrane proteins: An examination of differential light scattering and absorption flattening effects in large membrane vesicles and membrane sheets
    • B.A. Wallace, and D. Mao Circular dichroism analyses of membrane proteins: an examination of differential light scattering and absorption flattening effects in large membrane vesicles and membrane sheets Anal. Biochem. 142 1984 317 328
    • (1984) Anal. Biochem. , vol.142 , pp. 317-328
    • Wallace, B.A.1    Mao, D.2
  • 47
    • 0023652252 scopus 로고
    • Differential absorption flattening optical effects are significant in the circular dichroism spectra of large membrane fragments
    • B.A. Wallace, and C.L. Teeters Differential absorption flattening optical effects are significant in the circular dichroism spectra of large membrane fragments Biochemistry 26 1987 65 70
    • (1987) Biochemistry , vol.26 , pp. 65-70
    • Wallace, B.A.1    Teeters, C.L.2
  • 50
    • 0029997936 scopus 로고    scopus 로고
    • Protein purification in the nineties
    • R.K. Scopes Protein purification in the nineties Biotechnol. Appl. Biochem. 23 1996 197 204
    • (1996) Biotechnol. Appl. Biochem. , vol.23 , pp. 197-204
    • Scopes, R.K.1
  • 51
    • 0020477017 scopus 로고
    • Stabilization of protein structure by sugars
    • T. Arakawa, and S.N. Timasheff Stabilization of protein structure by sugars Biochemistry 21 1982 6536 6544
    • (1982) Biochemistry , vol.21 , pp. 6536-6544
    • Arakawa, T.1    Timasheff, S.N.2
  • 52
    • 4344614677 scopus 로고    scopus 로고
    • Effects of naturally occurring osmolytes on protein stability and solubility: Issues important in protein crystallization
    • D.W. Bolen Effects of naturally occurring osmolytes on protein stability and solubility: issues important in protein crystallization Methods 34 2004 312 322
    • (2004) Methods , vol.34 , pp. 312-322
    • Bolen, D.W.1
  • 56
    • 0021112596 scopus 로고
    • Free energy changes in ribonuclease a denaturation. Effect of urea, guanidine hydrochloride, and lithium salts
    • F. Ahmad Free energy changes in ribonuclease A denaturation. Effect of urea, guanidine hydrochloride, and lithium salts J. Biol. Chem. 258 1983 11143 11146
    • (1983) J. Biol. Chem. , vol.258 , pp. 11143-11146
    • Ahmad, F.1
  • 57
    • 0027247584 scopus 로고
    • Perchlorate-induced denaturation of ribonuclease A: Investigation of possible folding intermediates
    • J.M. Scholtz, and R.L. Baldwin Perchlorate-induced denaturation of ribonuclease A: investigation of possible folding intermediates Biochemistry 32 1993 4604 4608
    • (1993) Biochemistry , vol.32 , pp. 4604-4608
    • Scholtz, J.M.1    Baldwin, R.L.2
  • 58
  • 59
    • 0017109004 scopus 로고
    • Conformational properties of the complexes formed by proteins and sodium dodecyl sulfate
    • W.L. Mattice, J.M. Riser, and D.S. Clark Conformational properties of the complexes formed by proteins and sodium dodecyl sulfate Biochemistry 15 1976 4264 4272
    • (1976) Biochemistry , vol.15 , pp. 4264-4272
    • Mattice, W.L.1    Riser, J.M.2    Clark, D.S.3
  • 60
    • 0017175473 scopus 로고
    • Conformational transitions of non-helical proteins effected by dodecyl sulfate. Circular dichroism of alpha1-acid glycoprotein, Bence Jones protein, carbonic anhydrase B, deoxyribonuclease, pepsinogen, and plasminogen
    • B. Jirgensons Conformational transitions of non-helical proteins effected by dodecyl sulfate. Circular dichroism of alpha1-acid glycoprotein, Bence Jones protein, carbonic anhydrase B, deoxyribonuclease, pepsinogen, and plasminogen Biochim. Biophys. Acta 434 1976 58 68
    • (1976) Biochim. Biophys. Acta , vol.434 , pp. 58-68
    • Jirgensons, B.1
  • 61
    • 0032444658 scopus 로고    scopus 로고
    • Trifluoroethanol and colleagues: Cosolvents come of age
    • M. Buck Trifluoroethanol and colleagues: cosolvents come of age Q. Rev. Biophys. 31 1998 297 355
    • (1998) Q. Rev. Biophys. , vol.31 , pp. 297-355
    • Buck, M.1
  • 62
    • 11844262057 scopus 로고    scopus 로고
    • Spectroscopic evidence for backbone desolvation of helical peptides by 2,2,2-trifluoroethanol: An isotope-edited FTIR study
    • A. Starzyk, W. Barber-Armstrong, M. Sridharan, and S.M. Decatur Spectroscopic evidence for backbone desolvation of helical peptides by 2,2,2-trifluoroethanol: an isotope-edited FTIR study Biochemistry 44 2005 369 376
    • (2005) Biochemistry , vol.44 , pp. 369-376
    • Starzyk, A.1    Barber-Armstrong, W.2    Sridharan, M.3    Decatur, S.M.4
  • 64
    • 0016160429 scopus 로고
    • Measurement of protein by spectrophotometry at 205 nm
    • R.K. Scopes Measurement of protein by spectrophotometry at 205 nm Anal. Biochem. 59 1974 277 282
    • (1974) Anal. Biochem. , vol.59 , pp. 277-282
    • Scopes, R.K.1
  • 65
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • S.C. Gill, and P.H. von Hippel Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182 1989 319 326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 66
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • C.N. Pace, F. Vajdos, L. Fee, G. Grimsley, and T. Gray How to measure and predict the molar absorption coefficient of a protein Prot. Sci. 4 1995 2411 2423
    • (1995) Prot. Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 67
    • 0026585599 scopus 로고
    • Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins
    • H. Mach, C.R. Middaugh, and R.V. Lewis Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins Anal. Biochem. 200 1992 74 80
    • (1992) Anal. Biochem. , vol.200 , pp. 74-80
    • MacH, H.1    Middaugh, C.R.2    Lewis, R.V.3
  • 68
    • 0348147599 scopus 로고    scopus 로고
    • Calibration and standardisation of synchrotron radiation circular dichroism and conventional circular dichroism spectrophotometers
    • A.J. Miles, F. Wien, J.G. Lees, A. Rodger, R.W. Janes, and B.A. Wallace Calibration and standardisation of synchrotron radiation circular dichroism and conventional circular dichroism spectrophotometers Spectroscopy 17 2003 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
  • 70
    • 0000814919 scopus 로고
    • Direct determination of absolute circular dichroism data and calibration of commercial instruments
    • P.H. Schippers, and H.P.J.M. Dekkers Direct determination of absolute circular dichroism data and calibration of commercial instruments Anal. Chem. 53 1981 778 782
    • (1981) Anal. Chem. , vol.53 , pp. 778-782
    • Schippers, P.H.1    Dekkers, H.P.J.M.2
  • 71
    • 12844253803 scopus 로고    scopus 로고
    • Calibration and standardisation of synchrotron radiation circular dichroism and conventional circular dichroism spectrophotometers. Part 2: Factors affecting magnitude and wavelength
    • A.J. Miles, F. Wien, J.G. Lees, and B.A. Wallace Calibration and standardisation of synchrotron radiation circular dichroism and conventional circular dichroism spectrophotometers. Part 2: factors affecting magnitude and wavelength Spectroscopy 19 2005 43 51
    • (2005) Spectroscopy , vol.19 , pp. 43-51
    • Miles, A.J.1    Wien, F.2    Lees, J.G.3    Wallace, B.A.4
  • 72
    • 8844221903 scopus 로고    scopus 로고
    • Redetermination of the extinction coefficient of camphor-10-sulfonic acid, a calibration standard for circular dichroism spectroscopy
    • A.J. Miles, F. Wien, and B.A. Wallace Redetermination of the extinction coefficient of camphor-10-sulfonic acid, a calibration standard for circular dichroism spectroscopy Anal. Biochem. 335 2004 338 339
    • (2004) Anal. Biochem. , vol.335 , pp. 338-339
    • Miles, A.J.1    Wien, F.2    Wallace, B.A.3
  • 73
    • 0020184861 scopus 로고
    • Experimental errors and their effect on analysing circular dichroism spectra of proteins
    • J.P. Hennessey Jr., and W.C. Johnson Jr. Experimental errors and their effect on analysing circular dichroism spectra of proteins Anal. Biochem. 125 1982 177 188
    • (1982) Anal. Biochem. , vol.125 , pp. 177-188
    • Hennessey Jr., J.P.1    Johnson Jr., W.C.2
  • 74
    • 0000841214 scopus 로고
    • An alkaline solution of potassium chromate as a transmittancy standard in the ultraviolet
    • G.W. Haupt An alkaline solution of potassium chromate as a transmittancy standard in the ultraviolet J. Res. Natl. Bur. Stand. 48 1952 414 423
    • (1952) J. Res. Natl. Bur. Stand. , vol.48 , pp. 414-423
    • Haupt, G.W.1
  • 75
    • 0025155512 scopus 로고
    • Folding transition in the DNA-binding domain of GCN4 on specific binding to DNA
    • M.A. Weiss, T. Ellenberger, C.R. Wobbe, J.P. Lee, S.C. Harrison, and K. Struhl Folding transition in the DNA-binding domain of GCN4 on specific binding to DNA Nature 347 1990 575 578
    • (1990) Nature , vol.347 , pp. 575-578
    • Weiss, M.A.1    Ellenberger, T.2    Wobbe, C.R.3    Lee, J.P.4    Harrison, S.C.5    Struhl, K.6
  • 76
    • 0028783624 scopus 로고
    • Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy
    • J.A. Zitzewitz, O. Bilsel, J. Luo, B.E. Jones, and C.R. Matthews Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy Biochemistry 34 1995 12812 12819
    • (1995) Biochemistry , vol.34 , pp. 12812-12819
    • Zitzewitz, J.A.1    Bilsel, O.2    Luo, J.3    Jones, B.E.4    Matthews, C.R.5
  • 77
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • W.C. Johnson Jr. Protein secondary structure and circular dichroism: a practical guide Proteins: Struct. Funct. Genet. 7 1990 205 214
    • (1990) Proteins: Struct. Funct. Genet. , vol.7 , pp. 205-214
    • Johnson Jr., W.C.1
  • 78
    • 4644319196 scopus 로고    scopus 로고
    • CDtool-an integrated software package for circular dichroism spectroscopic data processing, analysis and archiving
    • J.G. Lees, B.R. Smith, F. Wien, A.J. Miles, and B.A. Wallace CDtool-an integrated software package for circular dichroism spectroscopic data processing, analysis and archiving Anal. Biochem. 332 2004 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
  • 79
    • 33644577717 scopus 로고    scopus 로고
    • PhD Thesis, University of London
    • J.G. Lees, PhD Thesis, University of London (2005).
    • (2005)
    • Lees, J.G.1
  • 80
    • 3242742115 scopus 로고    scopus 로고
    • The optimization of protein secondary structure determination with infrared and circular dichroism spectra
    • K.A. Oberg, J.-M. Ruysschaert, and E. Goormaghtigh The optimization of protein secondary structure determination with infrared and circular dichroism spectra Eur. J. Biochem. 271 2004 2937 2948
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2937-2948
    • Oberg, K.A.1    Ruysschaert, J.-M.2    Goormaghtigh, E.3
  • 82
    • 73049144001 scopus 로고
    • The far ultraviolet absorption spectra of polypeptide and protein solutions and their dependence on conformation
    • K. Rosenheck, and P. Doty The far ultraviolet absorption spectra of polypeptide and protein solutions and their dependence on conformation Proc. Natl. Acad. Sci. U. S. A. 47 1961 1775 1785
    • (1961) Proc. Natl. Acad. Sci. U. S. A. , vol.47 , pp. 1775-1785
    • Rosenheck, K.1    Doty, P.2
  • 83
    • 0000248275 scopus 로고
    • Ultraviolet absorption spectra of some inorganic ions in aqueous solutions
    • R.P. Buck, S. Singhadeja, and L.B. Rogers Ultraviolet absorption spectra of some inorganic ions in aqueous solutions Anal. Chem. 26 1954 1240 1242
    • (1954) Anal. Chem. , vol.26 , pp. 1240-1242
    • Buck, R.P.1    Singhadeja, S.2    Rogers, L.B.3
  • 84
    • 0029769521 scopus 로고    scopus 로고
    • Localization of the active site of type II dehydroquinases. Identification of a common arginine-containing motif in the two classes of dehydroquinases
    • T. Krell, M.J. Horsburgh, A. Cooper, S.M. Kelly, and J.R. Coggins Localization of the active site of type II dehydroquinases. Identification of a common arginine-containing motif in the two classes of dehydroquinases J. Biol. Chem. 271 1996 24492 24497
    • (1996) J. Biol. Chem. , vol.271 , pp. 24492-24497
    • Krell, T.1    Horsburgh, M.J.2    Cooper, A.3    Kelly, S.M.4    Coggins, J.R.5
  • 85
    • 0030917717 scopus 로고    scopus 로고
    • Characterisation of the molybdenum-responsive ModE regulatory protein and its binding to the promoter region of the modABCD (molybdenum transport) operon of Escherichia coli
    • L.A. Anderson, T. Palmer, N.C. Price, S. Bornemann, D.H. Boxer, and R.N. Pau Characterisation of the molybdenum-responsive ModE regulatory protein and its binding to the promoter region of the modABCD (molybdenum transport) operon of Escherichia coli Eur. J. Biochem. 246 1997 119 126
    • (1997) Eur. J. Biochem. , vol.246 , pp. 119-126
    • Anderson, L.A.1    Palmer, T.2    Price, N.C.3    Bornemann, S.4    Boxer, D.H.5    Pau, R.N.6


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