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Volumn 1, Issue 6, 2007, Pages 2876-2890

Using circular dichroism spectra to estimate protein secondary structure

Author keywords

[No Author keywords available]

Indexed keywords

BUFFER; PEPTIDE; PROTEIN;

EID: 34548847733     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2006.202     Document Type: Article
Times cited : (2939)

References (65)
  • 2
    • 0014009972 scopus 로고
    • Circular dichroism of biological macromolecules
    • Beychok, S. Circular dichroism of biological macromolecules. Science 154, 1288-1299 (1966).
    • (1966) Science , vol.154 , pp. 1288-1299
    • Beychok, S.1
  • 3
    • 1642546383 scopus 로고    scopus 로고
    • Computation and analysis of protein circular dichroism spectra
    • Sreerama, N. & Woody, R.W. Computation and analysis of protein circular dichroism spectra. Methods Enzymol. 383, 318-351 (2004).
    • (2004) Methods Enzymol , vol.383 , pp. 318-351
    • Sreerama, N.1    Woody, R.W.2
  • 4
    • 11344291497 scopus 로고
    • The ultraviolet circular dichroism of polypeptides
    • Holzwarth, G. & Doty, P. The ultraviolet circular dichroism of polypeptides. J. Am. Chem. Soc. 87, 218-228 (1965).
    • (1965) J. Am. Chem. Soc , vol.87 , pp. 218-228
    • Holzwarth, G.1    Doty, P.2
  • 5
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N. & Fasman, G.D. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8, 4108-4116 (1969).
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 6
    • 0027501381 scopus 로고
    • Circular dichroic analysis of denatured proteins: Inclusion of denatured proteins in the reference set
    • Venyaminov, S., Baikalov, I.A., Shen, Z.M., Wu, C.S. & Yang, J.T. Circular dichroic analysis of denatured proteins: Inclusion of denatured proteins in the reference set. Anal. Biochem. 214, 17-24 (1993).
    • (1993) Anal. Biochem , vol.214 , pp. 17-24
    • Venyaminov, S.1    Baikalov, I.A.2    Shen, Z.M.3    Wu, C.S.4    Yang, J.T.5
  • 7
    • 84984084816 scopus 로고
    • Circular dichroism spectrum of poly-L-proline
    • Bovey, F.A. & Hood, F.P. Circular dichroism spectrum of poly-L-proline. Biopolymers 5, 325-326 (1967).
    • (1967) Biopolymers , vol.5 , pp. 325-326
    • Bovey, F.A.1    Hood, F.P.2
  • 8
    • 0015455860 scopus 로고
    • Effect of temperature on the circular dichroism spectra of polypeptides in the extended state
    • Tiffany, M.L. & Krimm, S. Effect of temperature on the circular dichroism spectra of polypeptides in the extended state. Biopolymers 11, 2309-2316 (1972).
    • (1972) Biopolymers , vol.11 , pp. 2309-2316
    • Tiffany, M.L.1    Krimm, S.2
  • 9
    • 0002251831 scopus 로고
    • Circular dichroism and conformation of unordered polypeptides
    • Woody, R.W. Circular dichroism and conformation of unordered polypeptides. Adv. Biophys. Chem. 2, 31-79 (1992).
    • (1992) Adv. Biophys. Chem , vol.2 , pp. 31-79
    • Woody, R.W.1
  • 10
    • 0036129072 scopus 로고    scopus 로고
    • Polyproline II helical structure in protein unfolded states: Lysine peptides revisited
    • Rucker, A.L. & Creamer, T.P. Polyproline II helical structure in protein unfolded states: Lysine peptides revisited. Protein Sci. 11, 980-985 (2002).
    • (2002) Protein Sci , vol.11 , pp. 980-985
    • Rucker, A.L.1    Creamer, T.P.2
  • 11
    • 0030628997 scopus 로고    scopus 로고
    • Infrared and Raman vibrational optical activity: Theoretical and experimental aspects
    • Nafie, L.A. Infrared and Raman vibrational optical activity: Theoretical and experimental aspects. Annu. Rev. Phys. Chem. 48, 357-386 (1997).
    • (1997) Annu. Rev. Phys. Chem , vol.48 , pp. 357-386
    • Nafie, L.A.1
  • 12
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • Jackson, M. & Mantsch, H.H. The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 30, 95-120 (1995).
    • (1995) Crit. Rev. Biochem. Mol. Biol , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 13
    • 0029438076 scopus 로고
    • Fourier transform infrared spectroscopy investigations of protein structure
    • Cooper, E.A. & Knutson, K. Fourier transform infrared spectroscopy investigations of protein structure. Pharm. Biotechnol. 7, 101-143 (1995).
    • (1995) Pharm. Biotechnol , vol.7 , pp. 101-143
    • Cooper, E.A.1    Knutson, K.2
  • 14
    • 0034650323 scopus 로고    scopus 로고
    • Spectroscopic methods for analysis of protein secondary structure
    • Pelton, J.T. & McLean, L.R. Spectroscopic methods for analysis of protein secondary structure. Anal. Biochem. 277, 167-176 (2000).
    • (2000) Anal. Biochem , vol.277 , pp. 167-176
    • Pelton, J.T.1    McLean, L.R.2
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254 (1976).
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0019871893 scopus 로고
    • Information content in the circular dichroism of proteins
    • Hennessey, J.P. Jr. & Johnson, W.C. Jr. Information content in the circular dichroism of proteins. Biochemistry 20, 1085-1094 (1981).
    • (1981) Biochemistry , vol.20 , pp. 1085-1094
    • Hennessey Jr., J.P.1    Johnson Jr., W.C.2
  • 18
    • 33947463042 scopus 로고
    • Simple microdetermination of Kjeldahl nitrogen in biological material
    • Lang, C.A. Simple microdetermination of Kjeldahl nitrogen in biological material. Anal. Chem. 30, 1692-1694 (1958).
    • (1958) Anal. Chem , vol.30 , pp. 1692-1694
    • Lang, C.A.1
  • 19
    • 0016279769 scopus 로고
    • A rapid micromethod for the determination of nitrogen and phosphate in biological material
    • Jaenicke, L. A rapid micromethod for the determination of nitrogen and phosphate in biological material. Anal. Biochem. 61, 623-627 (1974).
    • (1974) Anal. Biochem , vol.61 , pp. 623-627
    • Jaenicke, L.1
  • 20
    • 0019005874 scopus 로고
    • Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism
    • Brahms, S. & Brahms, J. Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism. J. Mol. Biol. 138, 149-178 (1980).
    • (1980) J. Mol. Biol , vol.138 , pp. 149-178
    • Brahms, S.1    Brahms, J.2
  • 21
    • 0031543338 scopus 로고    scopus 로고
    • A set of constructed type spectra for the practical estimation of peptide secondary structure from circular dichroism
    • Reed, J. & Reed, T.A. A set of constructed type spectra for the practical estimation of peptide secondary structure from circular dichroism. Anal. Biochem. 254, 36-40 (1997).
    • (1997) Anal. Biochem , vol.254 , pp. 36-40
    • Reed, J.1    Reed, T.A.2
  • 22
    • 0015057050 scopus 로고
    • A new basis for interpreting the circular dichroic spectra of proteins
    • Saxena, V.P. & Wetlaufer, D.B. A new basis for interpreting the circular dichroic spectra of proteins. Proc. Natl Acad. Sci. USA 68, 969-972 (1971).
    • (1971) Proc. Natl Acad. Sci. USA , vol.68 , pp. 969-972
    • Saxena, V.P.1    Wetlaufer, D.B.2
  • 23
    • 0016169865 scopus 로고
    • Determination of the helix and β form of proteins in aqueous solution by circular dichroism
    • Chen, Y.H., Yang, J.T. & Chau, K.H. Determination of the helix and β form of proteins in aqueous solution by circular dichroism. Biochemistry 13, 3350-3359 (1974).
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3
  • 24
    • 0018118041 scopus 로고
    • Circular dichroic analysis of protein conformation: Inclusion of the β-turns
    • Chang, C.T., Wu, C.S. & Yang, J.T. Circular dichroic analysis of protein conformation: Inclusion of the β-turns. Anal. Biochem. 91, 13-31 (1978).
    • (1978) Anal. Biochem , vol.91 , pp. 13-31
    • Chang, C.T.1    Wu, C.S.2    Yang, J.T.3
  • 25
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang, J.T., Wu, C.S. & Martinez, H.M. Calculation of protein conformation from circular dichroism. Methods Enzymol. 130, 208-269 (1986).
    • (1986) Methods Enzymol , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.S.2    Martinez, H.M.3
  • 26
    • 0030042763 scopus 로고    scopus 로고
    • Methods to estimate the conformation of proteins and polypeptides from circular dichroism data
    • Greenfield, N.J. Methods to estimate the conformation of proteins and polypeptides from circular dichroism data. Anal. Biochem. 235 1-10 (1996).
    • (1996) Anal. Biochem , vol.235 , pp. 1-10
    • Greenfield, N.J.1
  • 27
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher, S.W. & Glöckner, J. Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20 33-37 (1981).
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glöckner, J.2
  • 28
    • 0023656828 scopus 로고
    • Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra
    • Manavalan, P. & Johnson, W.C. Jr. Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal. Biochem. 167, 76-85 (1987).
    • (1987) Anal. Biochem , vol.167 , pp. 76-85
    • Manavalan, P.1    Johnson Jr., W.C.2
  • 29
    • 0026599616 scopus 로고
    • Extending CD spectra of proteins to 168 nm improves the analysis for secondary structures
    • Toumadje, A., Alcorn, S.W. & Johnson, W.C. Jr. Extending CD spectra of proteins to 168 nm improves the analysis for secondary structures. Anal. Biochem. 200, 321-331 (1992).
    • (1992) Anal. Biochem , vol.200 , pp. 321-331
    • Toumadje, A.1    Alcorn, S.W.2    Johnson Jr., W.C.3
  • 30
    • 0027199881 scopus 로고
    • Effects of relative band intensity on prediction of protein secondary structure from CD
    • Toumadje, A. & Johnson, W.C. Jr. Effects of relative band intensity on prediction of protein secondary structure from CD. Anal. Biochem. 211, 258-260 (1993).
    • (1993) Anal. Biochem , vol.211 , pp. 258-260
    • Toumadje, A.1    Johnson Jr., W.C.2
  • 31
    • 0033562629 scopus 로고    scopus 로고
    • Analyzing protein circular dichroism spectra for accurate secondary structures
    • Johnson, W.C. Analyzing protein circular dichroism spectra for accurate secondary structures. Proteins 35, 307-312 (1999).
    • (1999) Proteins , vol.35 , pp. 307-312
    • Johnson, W.C.1
  • 32
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • Sreerama, N. & Woody, R.W. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 209, 32-44 (1993).
    • (1993) Anal. Biochem , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 33
    • 0027988296 scopus 로고
    • Protein secondary structure from circular dichroism spectroscopy. Combining variable selection principle and cluster analysis with neural network, ridge regression and self-consistent methods
    • Sreerama, N. & Woody, R.W. Protein secondary structure from circular dichroism spectroscopy. Combining variable selection principle and cluster analysis with neural network, ridge regression and self-consistent methods. J. Mol. Biol. 242, 497-507 (1994).
    • (1994) J. Mol. Biol , vol.242 , pp. 497-507
    • Sreerama, N.1    Woody, R.W.2
  • 34
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of α-helical and β-strand segments in proteins using circular dichroism spectroscopy
    • Sreerama, N., Venyaminov, S.Y. & Woody, R.W. Estimation of the number of α-helical and β-strand segments in proteins using circular dichroism spectroscopy. Protein Sci. 8, 370-380 (1999).
    • (1999) Protein Sci , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 35
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Inclusion of denatured proteins with native proteins in the analysis
    • Sreerama, N., Venyaminov, S.Y. & Woody, R.W. Estimation of protein secondary structure from circular dichroism spectra: Inclusion of denatured proteins with native proteins in the analysis. Anal. Biochem. 287, 243-251 (2000).
    • (2000) Anal. Biochem , vol.287 , pp. 243-251
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 36
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N. & Woody, R.W. Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287, 252-260 (2000).
    • (2000) Anal. Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 37
    • 0026530383 scopus 로고
    • Quantitative analysis of protein far UV circular dichroism spectra by neural networks
    • Böhm, G., Muhr, R. & Jaenicke, R. Quantitative analysis of protein far UV circular dichroism spectra by neural networks. Protein Eng. 5, 191-195 (1992).
    • (1992) Protein Eng , vol.5 , pp. 191-195
    • Böhm, G.1    Muhr, R.2    Jaenicke, R.3
  • 38
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network
    • Andrade, M.A., Chacón, P., Merelo, J.J. & Morán, F. Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng. 6, 383-390 (1993).
    • (1993) Protein Eng , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacón, P.2    Merelo, J.J.3    Morán, F.4
  • 39
    • 0035283168 scopus 로고    scopus 로고
    • SOMCD: Method for evaluating protein secondary structure from UV circular dichroism spectra
    • Unneberg, P., Merelo, J.J., Chacón, P. & Morán, F. SOMCD: Method for evaluating protein secondary structure from UV circular dichroism spectra. Proteins 42, 460-470 (2001).
    • (2001) Proteins , vol.42 , pp. 460-470
    • Unneberg, P.1    Merelo, J.J.2    Chacón, P.3    Morán, F.4
  • 40
    • 0026696116 scopus 로고
    • Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: A practical guide
    • Perczel, A., Park, K. & Fasman, G.D. Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: A practical guide. Anal. Biochem. 203, 83-93 (1992).
    • (1992) Anal. Biochem , vol.203 , pp. 83-93
    • Perczel, A.1    Park, K.2    Fasman, G.D.3
  • 41
    • 0015230487 scopus 로고
    • A new approach to the calculation of secondary structures of globular proteins by optical rotatory dispersion and circular dichroism
    • Chen, Y.H. & Yang, J.T. A new approach to the calculation of secondary structures of globular proteins by optical rotatory dispersion and circular dichroism. Biochem. Biophys. Res. Commun. 44, 1285-1291 (1971).
    • (1971) Biochem. Biophys. Res. Commun , vol.44 , pp. 1285-1291
    • Chen, Y.H.1    Yang, J.T.2
  • 42
    • 0015522150 scopus 로고
    • Determination of the secondary structures of proteins by circular dichroismand optical rotatory dispersion
    • Chen, Y.H., Yang, J.T. & Martinez, H.M. Determination of the secondary structures of proteins by circular dichroismand optical rotatory dispersion. Biochemistry 11, 4120-4131 (1972).
    • (1972) Biochemistry , vol.11 , pp. 4120-4131
    • Chen, Y.H.1    Yang, J.T.2    Martinez, H.M.3
  • 43
    • 0027932724 scopus 로고
    • Poly(pro)II helices in globular proteins: Identification and circular dichroic analysis
    • Sreerama, N. & Woody, R.W. Poly(pro)II helices in globular proteins: identification and circular dichroic analysis. Biochemistry 33 10022-10025 (1994).
    • (1994) Biochemistry , vol.33 , pp. 10022-10025
    • Sreerama, N.1    Woody, R.W.2
  • 44
    • 0025861478 scopus 로고
    • Convex constraint analysis: A natural deconvolution of circular dichroism curves of proteins
    • Perczel, A., Hollósi, M., Tusnády, G. & Fasman, G.D. Convex constraint analysis: A natural deconvolution of circular dichroism curves of proteins. Protein Eng. 4, 669-679 (1991).
    • (1991) Protein Eng , vol.4 , pp. 669-679
    • Perczel, A.1    Hollósi, M.2    Tusnády, G.3    Fasman, G.D.4
  • 45
    • 0027265825 scopus 로고
    • Conformational intermediates in the folding of a coiled-coil model peptide of the N-terminus of tropomyosin and α-tropomyosin
    • Greenfield, N.J. & Hitchcock-DeGregori, S.E. Conformational intermediates in the folding of a coiled-coil model peptide of the N-terminus of tropomyosin and α-tropomyosin. Protein Sci. 2 1263-1273 (1993).
    • (1993) Protein Sci , vol.2 , pp. 1263-1273
    • Greenfield, N.J.1    Hitchcock-DeGregori, S.E.2
  • 46
    • 0027363495 scopus 로고
    • Thermal stability and conformational transitions of scrapie amyloid (prion) protein correlate with infectivity
    • Safar, J., Roller, P.P., Gajdusek, D.C. & Gibbs, C.J. Jr. Thermal stability and conformational transitions of scrapie amyloid (prion) protein correlate with infectivity. Protein Sci. 2, 2206-2216 (1993).
    • (1993) Protein Sci , vol.2 , pp. 2206-2216
    • Safar, J.1    Roller, P.P.2    Gajdusek, D.C.3    Gibbs Jr., C.J.4
  • 47
    • 34548819311 scopus 로고    scopus 로고
    • Using circular dichroism, collected as a function of temperature, to determine the thermodynamics of protein unfolding and binding interactions
    • doi: 10.1038/nprot.2006.204
    • Greenfield, N.J. Using circular dichroism, collected as a function of temperature, to determine the thermodynamics of protein unfolding and binding interactions. Nat. Protoc. doi: 10.1038/nprot.2006.204 (2006).
    • (2006) Nat. Protoc
    • Greenfield, N.J.1
  • 48
    • 0015870378 scopus 로고
    • Circular dichroism and optical rotatory dispersion of proteins and polypeptides
    • Adler, A.J., Greenfield, N.J. & Fasman, G.D. Circular dichroism and optical rotatory dispersion of proteins and polypeptides. Methods Enzymol. 27, 675-735 (1973).
    • (1973) Methods Enzymol , vol.27 , pp. 675-735
    • Adler, A.J.1    Greenfield, N.J.2    Fasman, G.D.3
  • 49
    • 0016065880 scopus 로고
    • Circular dichroism of helical and nonhelical proteins. A review of the limits of the methods for calculating secondary structure
    • Rosenkranz, H. Circular dichroism of helical and nonhelical proteins. A review of the limits of the methods for calculating secondary structure. Z. Klin. Chem. Klin. Biochem. 12, 222 (1974).
    • (1974) Z. Klin. Chem. Klin. Biochem , vol.12 , pp. 222
    • Rosenkranz, H.1
  • 50
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Johnson, W.C. Jr. Protein secondary structure and circular dichroism: A practical guide. Proteins 7, 205-214 (1990).
    • (1990) Proteins , vol.7 , pp. 205-214
    • Johnson Jr., W.C.1
  • 51
    • 0028959773 scopus 로고
    • Circular dichroism
    • Woody, R.W. Circular dichroism. Methods Enzymol. 246, 34-71 (1995).
    • (1995) Methods Enzymol , vol.246 , pp. 34-71
    • Woody, R.W.1
  • 52
  • 53
    • 33644873189 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism spectroscopy of proteins and applications in structural and functional genomics
    • Miles, A.J. & Wallace, B.A. Synchrotron radiation circular dichroism spectroscopy of proteins and applications in structural and functional genomics. Chem. Soc. Rev. 35, 39-51 (2006).
    • (2006) Chem. Soc. Rev , vol.35 , pp. 39-51
    • Miles, A.J.1    Wallace, B.A.2
  • 55
    • 34548817291 scopus 로고    scopus 로고
    • Determination of the folding of proteins as a function of denaturants, osmolytes or ligands using circular dichroism
    • doi: 10.1038/nprot.2006.229
    • Greenfield, N.J. Determination of the folding of proteins as a function of denaturants, osmolytes or ligands using circular dichroism. Nat. Protoc. doi: 10.1038/nprot.2006.229 (2006).
    • (2006) Nat. Protoc
    • Greenfield, N.J.1
  • 56
    • 34548864513 scopus 로고    scopus 로고
    • The use of circular dichroism to study the kinetics of protein folding and unfolding
    • doi: 10.1038/ nprot.2006.244
    • Greenfield, N.J. The use of circular dichroism to study the kinetics of protein folding and unfolding. Nat. Protoc. doi: 10.1038/ nprot.2006.244 (2006).
    • (2006) Nat. Protoc
    • Greenfield, N.J.1
  • 57
    • 13244255213 scopus 로고    scopus 로고
    • Spectral magnitude effects on the analyses of secondary structure from circular dichroism spectroscopic data
    • Miles, A.J., Whitmore, L. & Wallace, B.A. Spectral magnitude effects on the analyses of secondary structure from circular dichroism spectroscopic data. Protein Sci. 14, 368-374 (2005).
    • (2005) Protein Sci , vol.14 , pp. 368-374
    • Miles, A.J.1    Whitmore, L.2    Wallace, B.A.3
  • 58
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6, 1948-1954 (1967).
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 59
    • 33947323296 scopus 로고
    • Numerical values of the absorbances of the aromatic amino acids in acid, neutral, and alkaline solutions
    • Mihalyi, E. Numerical values of the absorbances of the aromatic amino acids in acid, neutral, and alkaline solutions. J. Chem. Eng. Data 13, 179-182 (1968).
    • (1968) J. Chem. Eng. Data , vol.13 , pp. 179-182
    • Mihalyi, E.1
  • 60
    • 77049162117 scopus 로고
    • A micro biuret method for protein determination
    • Goa, J. A micro biuret method for protein determination. Scand. J. Clin. Lab. Invest. 5, 218-222 (1953).
    • (1953) Scand. J. Clin. Lab. Invest , vol.5 , pp. 218-222
    • Goa, J.1
  • 61
    • 0031976413 scopus 로고    scopus 로고
    • Conformational diversity of acid-denatured cytochrome c studied by a matrix analysis of far-UV CD spectra
    • Konno, T. Conformational diversity of acid-denatured cytochrome c studied by a matrix analysis of far-UV CD spectra. Protein Sci. 7, 975-982 (1998).
    • (1998) Protein Sci , vol.7 , pp. 975-982
    • Konno, T.1
  • 62
    • 0025152261 scopus 로고
    • Changes in secondary structure follow the dissociation of human insulin hexamers: A circular dichroism study
    • Melberg, S.G. & Johnson, W.C. Jr. Changes in secondary structure follow the dissociation of human insulin hexamers: A circular dichroism study. Proteins 8, 280-286 (1990).
    • (1990) Proteins , vol.8 , pp. 280-286
    • Melberg, S.G.1    Johnson Jr., W.C.2
  • 63
    • 0042553279 scopus 로고
    • Smoothing and dIfferentiation of data by simplified least squares procedures
    • Savitsky, A. & Golay, M.J.E. Smoothing and dIfferentiation of data by simplified least squares procedures. Anal. Chem. 36, 1627-1639 (1964).
    • (1964) Anal. Chem , vol.36 , pp. 1627-1639
    • Savitsky, A.1    Golay, M.J.E.2
  • 64
    • 0018256713 scopus 로고
    • Physical evidence for the assembly of A and B chains of human placental collagen in a single triple helix
    • Bentz, H., Bächinger, H.P., Glanville, R. & Kühn, K. Physical evidence for the assembly of A and B chains of human placental collagen in a single triple helix. Eur. J. Biochem. 92, 563-567 (1978).
    • (1978) Eur. J. Biochem , vol.92 , pp. 563-567
    • Bentz, H.1    Bächinger, H.P.2    Glanville, R.3    Kühn, K.4
  • 65
    • 0002944544 scopus 로고
    • Structural transitions of lysozyme
    • Steiner, R.F. Structural transitions of lysozyme. Biochim. Biophys. Acta 79, 51-63 (1964).
    • (1964) Biochim. Biophys. Acta , vol.79 , pp. 51-63
    • Steiner, R.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.