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Volumn 5, Issue 12, 1996, Pages 2479-2484

A comparative CD study of carbonic anhydrase isoenzymes with different number of tryptophans: Impact on calculation of secondary structure content

Author keywords

aromatic amino acids; bovine carbonic anhydrase III; human carbonic anhydrase I and II; structure

Indexed keywords

CARBONATE DEHYDRATASE; ISOENZYME;

EID: 0030479049     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560051210     Document Type: Article
Times cited : (18)

References (32)
  • 1
    • 0015496940 scopus 로고
    • Amino acid sequence of human erythrocyte carbonic anhydrase B
    • Andersson B, Nyman PO, Strid L. 1972. Amino acid sequence of human erythrocyte carbonic anhydrase B. Biochem Biophys Res Commun 48:670-677.
    • (1972) Biochem Biophys Res Commun , vol.48 , pp. 670-677
    • Andersson, B.1    Nyman, P.O.2    Strid, L.3
  • 2
    • 0014011566 scopus 로고
    • Optical rotatory dispersion and circular dichroism of human carbonic anhydrase B and C
    • Beychock S, Armstrong JM, Lindblow C, Edsall JT. 1966. Optical rotatory dispersion and circular dichroism of human carbonic anhydrase B and C. J Biol Chem 241:5150-5160.
    • (1966) J Biol Chem , vol.241 , pp. 5150-5160
    • Beychock, S.1    Armstrong, J.M.2    Lindblow, C.3    Edsall, J.T.4
  • 3
    • 0026348543 scopus 로고
    • Rapid ion-exchange chromatography for preparative separation of proteins. IV. Application to bovine carbonic anhydrase III from skeletal muscle
    • Borén K, Larsson M, Bergenhem N, Carlsson U. 1991. Rapid ion-exchange chromatography for preparative separation of proteins. IV. Application to bovine carbonic anhydrase III from skeletal muscle. J Chromatogr 588:139-145.
    • (1991) J Chromatogr , vol.588 , pp. 139-145
    • Borén, K.1    Larsson, M.2    Bergenhem, N.3    Carlsson, U.4
  • 4
    • 0016638515 scopus 로고
    • Paramagnetic and fluorescent probes attached to "buried" sulfhydryl groups in human carbonic anhydrases. Application to inhibitor binding, denaturation and refolding
    • Carlsson U, Aasa R, Henderson LE, Jonsson BH, Lindskog S. 1975. Paramagnetic and fluorescent probes attached to "buried" sulfhydryl groups in human carbonic anhydrases. Application to inhibitor binding, denaturation and refolding. Eur J Biochem 52:25-36.
    • (1975) Eur J Biochem , vol.52 , pp. 25-36
    • Carlsson, U.1    Aasa, R.2    Henderson, L.E.3    Jonsson, B.H.4    Lindskog, S.5
  • 5
    • 0015522150 scopus 로고
    • Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion
    • Chen YH, Yang JT, Martinez HM 1972. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 11:4120-4131
    • (1972) Biochemistry , vol.11 , pp. 4120-4131
    • Chen, Y.H.1    Yang, J.T.2    Martinez, H.M.3
  • 6
    • 0022474744 scopus 로고
    • Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication
    • Compton LA, Johnson WC Jr. 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
  • 7
    • 0021858737 scopus 로고
    • Purification and some properties of carbonic anhydrase from bovine skeletal muscle
    • Engberg P, Millqvist E, Pohl G, Lindskog S. 1985. Purification and some properties of carbonic anhydrase from bovine skeletal muscle. Arch Biochem Biophys 241:628-638.
    • (1985) Arch Biochem Biophys , vol.241 , pp. 628-638
    • Engberg, P.1    Millqvist, E.2    Pohl, G.3    Lindskog, S.4
  • 8
    • 0024218271 scopus 로고
    • Refined structure of human carbonic anhydrase II at 2.0 Å resolution
    • Eriksson AE, Jones TA, Liljas A. 1988. Refined structure of human carbonic anhydrase II at 2.0 Å resolution. Proteins Struct Funct Genet 4:274-282.
    • (1988) Proteins Struct Funct Genet , vol.4 , pp. 274-282
    • Eriksson, A.E.1    Jones, T.A.2    Liljas, A.3
  • 9
    • 0027215631 scopus 로고
    • Refined structure of bovine carbonic anhydrase III at 2.0 Å resolution
    • Eriksson AE, Liljas A. 1993. Refined structure of bovine carbonic anhydrase III at 2.0 Å resolution. Proteins Struct Funct Genet 16:29-42
    • (1993) Proteins Struct Funct Genet , vol.16 , pp. 29-42
    • Eriksson, A.E.1    Liljas, A.2
  • 10
    • 0027959547 scopus 로고
    • Assignment of the contribution of the tryptophan residues to the circular dichroism spectrum of human carbonic anhydrase II
    • Freskgård PO, Mårtensson LG, Jonasson P, Jonsson BH, Carlsson U. 1994. Assignment of the contribution of the tryptophan residues to the circular dichroism spectrum of human carbonic anhydrase II. Biochemistry 33:14281-14288.
    • (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
  • 11
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield N, Fasman GD. 1969. Computed circular dichroism spectra for the evaluation of protein conformation Biochemistry 8:4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 12
    • 0026463503 scopus 로고
    • Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes
    • Håkansson K, Carlsson M, Svensson LA, Liljas A. 1992. Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes. J Mol Biol 227:1192-1204.
    • (1992) J Mol Biol , vol.227 , pp. 1192-1204
    • Håkansson, K.1    Carlsson, M.2    Svensson, L.A.3    Liljas, A.4
  • 13
    • 0015542339 scopus 로고
    • Large-scale preparation of the human carbonic anhydrases
    • Henderson LE, Henriksson D. 1973. Large-scale preparation of the human carbonic anhydrases Anal Biochem 51:288-296.
    • (1973) Anal Biochem , vol.51 , pp. 288-296
    • Henderson, L.E.1    Henriksson, D.2
  • 14
    • 0017178810 scopus 로고
    • Primary structure of human carbonic anhydrase C
    • Henderson LE, Henriksson D, Nyman PO. 1976. Primary structure of human carbonic anhydrase C. J Biol Chem 251:5457-5463.
    • (1976) J Biol Chem , vol.251 , pp. 5457-5463
    • Henderson, L.E.1    Henriksson, D.2    Nyman, P.O.3
  • 15
    • 0020184861 scopus 로고
    • Experimental errors and their effect on analyzing circular dichroism spectra of proteins
    • Hennessey JP Jr, Johnson WC Jr. 1982 Experimental errors and their effect on analyzing circular dichroism spectra of proteins. Anal Biochem 125:177-188.
    • (1982) Anal Biochem , vol.125 , pp. 177-188
    • Hennessey Jr., J.P.1    Johnson Jr., W.C.2
  • 16
    • 0003160946 scopus 로고
    • Structure and evolutionary origins of the carbonic anhydrase multigene family
    • Dodgson SJ, Tashian RE, Gros G, Carter NE, eds. New York/London: Plenum Press
    • Hewett-Emmet D, Tashian RE. 1991. Structure and evolutionary origins of the carbonic anhydrase multigene family. In: Dodgson SJ, Tashian RE, Gros G, Carter NE, eds. The carbonic anhydrases: Cellular physiology and molecular genetics. New York/London: Plenum Press. pp 15-32.
    • (1991) The Carbonic Anhydrases: Cellular Physiology and Molecular Genetics , pp. 15-32
    • Hewett-Emmet, D.1    Tashian, R.E.2
  • 17
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Johnson WC Jr. 1990 Protein secondary structure and circular dichroism: A practical guide. Proteins Struct Funct Genet 7:205-214.
    • (1990) Proteins Struct Funct Genet , vol.7 , pp. 205-214
    • Johnson Jr., W.C.1
  • 18
    • 0002940291 scopus 로고
    • Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-Å resolution
    • Kannan KK, Notstrand B, Fridborg K, Lövgren S, Ohlsson A, Petef M. 1975. Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-Å resolution. Proc Nat Acad Sci USA 72:51-55.
    • (1975) Proc Nat Acad Sci USA , vol.72 , pp. 51-55
    • Kannan, K.K.1    Notstrand, B.2    Fridborg, K.3    Lövgren, S.4    Ohlsson, A.5    Petef, M.6
  • 19
    • 0017378545 scopus 로고
    • Carbon-13 nuclear magnetic resonance probe of active-she ionizations in human carbonic anhydrase B
    • Khalifah RG, Strader DJ, Bryant SH, Gibbons SM. 1977. Carbon-13 nuclear magnetic resonance probe of active-she ionizations in human carbonic anhydrase B. Biochemistry 16:2241-2247.
    • (1977) Biochemistry , vol.16 , pp. 2241-2247
    • Khalifah, R.G.1    Strader, D.J.2    Bryant, S.H.3    Gibbons, S.M.4
  • 20
    • 0023656828 scopus 로고
    • Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra
    • Manavalan P, Johnson WC Jr. 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
  • 21
    • 0023428747 scopus 로고
    • Theoretical determination of the CD of proteins containing closely packed antiparallel β-sheets
    • Manning MC, Woody RW. 1987. Theoretical determination of the CD of proteins containing closely packed antiparallel β-sheets. Biopolymers 26:1731-1752.
    • (1987) Biopolymers , vol.26 , pp. 1731-1752
    • Manning, M.C.1    Woody, R.W.2
  • 22
    • 0024464461 scopus 로고
    • Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor
    • Manning MC, Woody RW. 1989. Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor. Biochemistry 28:8609-8613
    • (1989) Biochemistry , vol.28 , pp. 8609-8613
    • Manning, M.C.1    Woody, R.W.2
  • 23
    • 84990646668 scopus 로고
    • Improved model for tyrosine and phenylalanine contributions to the protein circular dichroism spectra
    • Manning MC, Sreerama N, Woody RW. 1992. Improved model for tyrosine and phenylalanine contributions to the protein circular dichroism spectra. Biophys J 61:A347.
    • (1992) Biophys J , vol.61
    • Manning, M.C.1    Sreerama, N.2    Woody, R.W.3
  • 24
    • 0028966987 scopus 로고
    • Contribution of individual tryptophan residues to the fluorescence spectrum of native and denatured forms of human carbonic anhydrase II
    • Mårtensson LG, Jonasson P, Freskgård PO, Svensson M, Carlsson U, Jonsson BH. 1995. Contribution of individual tryptophan residues to the fluorescence spectrum of native and denatured forms of human carbonic anhydrase II. Biochemistry 34:1011-1021.
    • (1995) Biochemistry , vol.34 , pp. 1011-1021
    • Mårtensson, L.G.1    Jonasson, P.2    Freskgård, P.O.3    Svensson, M.4    Carlsson, U.5    Jonsson, B.H.6
  • 25
    • 0025861478 scopus 로고
    • Convex constraint analysis. A natural deconvolution of circular dichroism curves of proteins
    • Perczel A, Hollósi M, Tusnády G, Fasman GD. 1991. Convex constraint analysis. A natural deconvolution of circular dichroism curves of proteins. Protein Eng 4:669-679.
    • (1991) Protein Eng , vol.4 , pp. 669-679
    • Perczel, A.1    Hollósi, M.2    Tusnády, G.3    Fasman, G.D.4
  • 26
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher SW, 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
  • 27
    • 0015057050 scopus 로고
    • A new basis for interpreting the circular dichroic spectra of proteins
    • Saxena VP, Wetlaufer DB 1971. A new basis for interpreting the circular dichroic spectra of proteins. Proc Natl Acad Sci USA 68:969-972.
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 969-972
    • Saxena, V.P.1    Wetlaufer, D.B.2
  • 28
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • Sreerama N, Woody RW. 1993. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal Biochem 209:32-44.
    • (1993) Anal Biochem , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 29
    • 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 RW. 1994. 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) J Mol Biol , vol.242 , pp. 497-507
    • Sreerama, N.1    Woody, R.W.2
  • 30
    • 0015997959 scopus 로고
    • Aromatic contributions to circular dichroism spectra of proteins
    • Strickland EH. 1974. Aromatic contributions to circular dichroism spectra of proteins. CRC Crit Rev Biochem 2:113-174.
    • (1974) CRC Crit Rev Biochem , vol.2 , pp. 113-174
    • Strickland, E.H.1
  • 31
    • 0027527209 scopus 로고
    • Circular dichroism studies of barnase and its mutants: Characterization of the contribution of aromatic side chains
    • Vuilleumier S, Sancho J, Loewenthal R, Fersht AR. 1993. Circular dichroism studies of barnase and its mutants: Characterization of the contribution of aromatic side chains. Biochemistry 32:10303-10313.
    • (1993) Biochemistry , vol.32 , pp. 10303-10313
    • Vuilleumier, S.1    Sancho, J.2    Loewenthal, R.3    Fersht, A.R.4
  • 32
    • 0017822448 scopus 로고
    • Aromatic side-chain contributions to the far ultraviolet circular dichroism of peptides and proteins
    • Woody RW. 1978. Aromatic side-chain contributions to the far ultraviolet circular dichroism of peptides and proteins. Biopolymers 17:1451-1467.
    • (1978) Biopolymers , vol.17 , pp. 1451-1467
    • Woody, R.W.1


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