메뉴 건너뛰기




Volumn 84, Issue 5, 2007, Pages 1001-1008

A reference dataset for circular dichroism spectroscopy tailored for the βγ-crystallin lens proteins

Author keywords

cataract; circular dichroism (CD) spectroscopy; crystallin; mutation; secondary structure analysis; synchrotron radiation circular dichroism (SRCD)

Indexed keywords

BETA CRYSTALLIN; GAMMA CRYSTALLIN;

EID: 34247096110     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exer.2007.01.016     Document Type: Article
Times cited : (19)

References (42)
  • 1
    • 0037449145 scopus 로고    scopus 로고
    • High-resolution X-ray crystal structures of human γD-crystallin (1.25 Å) and the R58H mutant (1.15 Å) associated with aculeiform cataract
    • Basak A., Bateman O., Slingsby C., Pande A., Asherie N., Ogun O., Benedek G.B., and Pande J. High-resolution X-ray crystal structures of human γD-crystallin (1.25 Å) and the R58H mutant (1.15 Å) associated with aculeiform cataract. J. Mol. Biol. 328 (2003) 1137-1147
    • (2003) J. Mol. Biol. , vol.328 , pp. 1137-1147
    • Basak, A.1    Bateman, O.2    Slingsby, C.3    Pande, A.4    Asherie, N.5    Ogun, O.6    Benedek, G.B.7    Pande, J.8
  • 6
    • 14144250992 scopus 로고    scopus 로고
    • Contributions of hydrophobic domain interface interactions to the folding and stability of human gammaD-crystallin
    • Flaugh S.L., Kosinski-Collins M.S., and King J. Contributions of hydrophobic domain interface interactions to the folding and stability of human gammaD-crystallin. Protein Sci. 14 (2005) 569-581
    • (2005) Protein Sci. , vol.14 , pp. 569-581
    • Flaugh, S.L.1    Kosinski-Collins, M.S.2    King, J.3
  • 7
    • 23644457960 scopus 로고    scopus 로고
    • Interdomain side-chain interactions in human gammaD crystallin influencing folding and stability
    • Flaugh S.L., Kosinski-Collins M.S., and King J. Interdomain side-chain interactions in human gammaD crystallin influencing folding and stability. Protein Sci. 14 (2005) 2030-2043
    • (2005) Protein Sci. , vol.14 , pp. 2030-2043
    • Flaugh, S.L.1    Kosinski-Collins, M.S.2    King, J.3
  • 8
    • 0037181130 scopus 로고    scopus 로고
    • Conformational change and destabilization of cataract gammaC-crystallin T5P mutant
    • Fu L., and Liang J.J. Conformational change and destabilization of cataract gammaC-crystallin T5P mutant. FEBS Lett. 513 (2002) 213-216
    • (2002) FEBS Lett. , vol.513 , pp. 213-216
    • Fu, L.1    Liang, J.J.2
  • 9
    • 0036444208 scopus 로고    scopus 로고
    • Unfolding of human lens recombinant betaB2- and gammaC-crystallins
    • Fu L., and Liang J.J. Unfolding of human lens recombinant betaB2- and gammaC-crystallins. J. Struct. Biol. 139 (2002) 191-198
    • (2002) J. Struct. Biol. , vol.139 , pp. 191-198
    • Fu, L.1    Liang, J.J.2
  • 10
    • 11844274723 scopus 로고    scopus 로고
    • The native oligomeric organization of alpha-crystallin, is it necessary for its chaperone function?
    • Horwitz J., Huang Q., and Ding L. The native oligomeric organization of alpha-crystallin, is it necessary for its chaperone function?. Exp. Eye Res. 79 (2004) 817-821
    • (2004) Exp. Eye Res. , vol.79 , pp. 817-821
    • Horwitz, J.1    Huang, Q.2    Ding, L.3
  • 11
    • 28444482398 scopus 로고    scopus 로고
    • Bioinformatics analyses of circular dichroism protein reference databases
    • Janes R.W. Bioinformatics analyses of circular dichroism protein reference databases. Bioinformatics 21 (2005) 4230-4238
    • (2005) Bioinformatics , vol.21 , pp. 4230-4238
    • Janes, R.W.1
  • 12
    • 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 (1999) 307-312
    • (1999) Proteins , vol.35 , pp. 307-312
    • Johnson, W.C.1
  • 13
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 (1983) 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 14
    • 0037372175 scopus 로고    scopus 로고
    • In vitro unfolding, refolding, and polymerization of human gammaD crystallin, a protein involved in cataract formation
    • Kosinski-Collins M.S., and King J. In vitro unfolding, refolding, and polymerization of human gammaD crystallin, a protein involved in cataract formation. Protein Sci. 12 (2003) 480-490
    • (2003) Protein Sci. , vol.12 , pp. 480-490
    • Kosinski-Collins, M.S.1    King, J.2
  • 15
    • 0030513191 scopus 로고    scopus 로고
    • An eye lens protein-water structure: 1.2 Å resolution structure of γB-crystallin at 150K
    • Kumaraswamy V.S., Lindley P.F., Slingsby C., and Glover I.D. An eye lens protein-water structure: 1.2 Å resolution structure of γB-crystallin at 150K. Acta Crystallogr 52 (1996) 611-622
    • (1996) Acta Crystallogr , vol.52 , pp. 611-622
    • Kumaraswamy, V.S.1    Lindley, P.F.2    Slingsby, C.3    Glover, I.D.4
  • 16
    • 33644858451 scopus 로고    scopus 로고
    • Deamidation in human lens betaB2-crystallin destabilizes the dimer
    • Lampi K.J., Amyx K.K., Ahmann P., and Steel E.A. Deamidation in human lens betaB2-crystallin destabilizes the dimer. Biochemistry 45 (2006) 3146-3153
    • (2006) Biochemistry , vol.45 , pp. 3146-3153
    • Lampi, K.J.1    Amyx, K.K.2    Ahmann, P.3    Steel, E.A.4
  • 17
    • 33747855587 scopus 로고    scopus 로고
    • A reference database for circular dichroism spectroscopy covering fold and secondary structure space
    • Lees J.G., Miles A.J., Wien F., and Wallace B.A. A reference database for circular dichroism spectroscopy covering fold and secondary structure space. Bioinformatics 22 (2006) 1955-1962
    • (2006) Bioinformatics , vol.22 , pp. 1955-1962
    • Lees, J.G.1    Miles, A.J.2    Wien, F.3    Wallace, B.A.4
  • 18
    • 33845267726 scopus 로고    scopus 로고
    • Lees, J.G., Miles, A.J., Janes, R.W., Wallace, B.A., 2006b. Novel methods for secondary structure determination using low wavelength (VUV) circular dichroism spectroscopic data. BMC Bioinformatics 7, 507-516.
  • 19
    • 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. 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
  • 21
    • 25444524072 scopus 로고    scopus 로고
    • Interaction and biophysical properties of human lens Q155* betaB2-crystallin mutant
    • Liu B.F., and Liang J.J. Interaction and biophysical properties of human lens Q155* betaB2-crystallin mutant. Mol. Vis 11 (2005) 321-327
    • (2005) Mol. Vis , vol.11 , pp. 321-327
    • Liu, B.F.1    Liang, J.J.2
  • 22
    • 17744391285 scopus 로고    scopus 로고
    • Unfolding crystallins: the destabilizing role of a beta-hairpin cysteine in betaB2-crystallin by simulation and experiment
    • MacDonald J.T., Purkiss A.G., Smith M.A., Evans P., Goodfellow J.M., and Slingsby C. Unfolding crystallins: the destabilizing role of a beta-hairpin cysteine in betaB2-crystallin by simulation and experiment. Protein Sci. 14 (2005) 1282-1292
    • (2005) Protein Sci. , vol.14 , pp. 1282-1292
    • MacDonald, J.T.1    Purkiss, A.G.2    Smith, M.A.3    Evans, P.4    Goodfellow, J.M.5    Slingsby, C.6
  • 23
    • 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. 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
  • 25
    • 3242742115 scopus 로고    scopus 로고
    • The optimization of protein secondary structure determination with infrared and circular dichroism spectra
    • Oberg K.A., Ruysschaert J.M., and Goormaghtigh E. 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
  • 29
    • 0026628269 scopus 로고
    • Deconvolution of the circular dichroism spectra of proteins: the circular dichroism spectra of the antiparallel β-sheet in proteins
    • Perczel A., Park K., and Fasman G.D. Deconvolution of the circular dichroism spectra of proteins: the circular dichroism spectra of the antiparallel β-sheet in proteins. Proteins 13 (1992) 57-69
    • (1992) Proteins , vol.13 , pp. 57-69
    • Perczel, A.1    Park, K.2    Fasman, G.D.3
  • 30
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher S.W., and Glockner J. 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    Glockner, J.2
  • 32
    • 0344921403 scopus 로고    scopus 로고
    • Stability, homodimerization, and calcium-binding properties of a single, variant beta gamma-crystallin domain of the protein absent in melanoma 1 (AIM1)
    • Rajini B., Graham C., Wistow G., and Sharma Y. Stability, homodimerization, and calcium-binding properties of a single, variant beta gamma-crystallin domain of the protein absent in melanoma 1 (AIM1). Biochemistry 42 (2003) 4552-4559
    • (2003) Biochemistry , vol.42 , pp. 4552-4559
    • Rajini, B.1    Graham, C.2    Wistow, G.3    Sharma, Y.4
  • 34
    • 0021106995 scopus 로고
    • Structural homology of lens crystallins. III. Secondary structure estimation from circular dichroism and prediction from amino acid sequences
    • Siezen R.J., and Argos P. Structural homology of lens crystallins. III. Secondary structure estimation from circular dichroism and prediction from amino acid sequences. Biochim. Biophys. Acta 748 (1983) 56-67
    • (1983) Biochim. Biophys. Acta , vol.748 , pp. 56-67
    • Siezen, R.J.1    Argos, P.2
  • 35
    • 33947723561 scopus 로고    scopus 로고
    • Smith, M.A., Bateman, O.A., Jaenicke, R., Slingsby, C., 2007. Mutation of interfaces in domain swapped human βB2-crystallin. Protein Sci. (in press).
  • 36
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy
    • Sreerama N., Venyaminov S.Y., and Woody R.W. Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy. Protein Sci. 8 (1999) 370-380
    • (1999) Protein Sci. , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 37
    • 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., and 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 (2000) 243-251
    • (2000) Anal. Biochem , vol.287 , pp. 243-251
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 38
    • 0035894333 scopus 로고    scopus 로고
    • Analysis of protein circular dichroism spectra based on the tertiary structure classification
    • Sreerama N., Venyaminov S.Y., and Woody R.W. Analysis of protein circular dichroism spectra based on the tertiary structure classification. Anal. Biochem 299 (2001) 271-274
    • (2001) Anal. Biochem , vol.299 , pp. 271-274
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 39
    • 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., and 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 (2000) 252-260
    • (2000) Anal. Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 41
    • 30344485698 scopus 로고    scopus 로고
    • The Protein Circular Dichroism Data Bank (PCDDB): a bioinformatics and spectroscopic resource. Proteins Struct. Funct
    • Wallace B.A., Whitmore L., and Janes R.W. The Protein Circular Dichroism Data Bank (PCDDB): a bioinformatics and spectroscopic resource. Proteins Struct. Funct. Bioinf 62 (2006) 1-3
    • (2006) Bioinf , vol.62 , pp. 1-3
    • Wallace, B.A.1    Whitmore, L.2    Janes, R.W.3
  • 42
    • 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. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32 (2004) 668-673
    • (2004) Nucleic Acids Res. , vol.32 , pp. 668-673
    • Whitmore, L.1    Wallace, B.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.