메뉴 건너뛰기




Volumn 6, Issue 1, 2007, Pages 41-49

Conformational analysis of the blue-light sensing protein YtvA reveals a competitive interface for LOV–LOV dimerization and interdomain interactions

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; UNCLASSIFIED DRUG; YTVA PROTEIN;

EID: 33845993618     PISSN: 1474905X     EISSN: 14749092     Source Type: Journal    
DOI: 10.1039/b610375h     Document Type: Article
Times cited : (58)

References (72)
  • 1
    • 1642274684 scopus 로고    scopus 로고
    • The PAS fold: A redefinition of the PAS domain based upon structural prediction
    • M. H. Hefti K. J. Francoijs S. C. de Vries R. Dixon J. Vervoort The PAS fold: A redefinition of the PAS domain based upon structural prediction FEBS J. 2004 271 1198-1208.
    • (2004) FEBS J. , vol.271 , pp. 1198-1208
    • Hefti, M.H.1    Francoijs, K.J.2    de Vries, S.C.3    Dixon, R.4    Vervoort, J.5
  • 3
    • 0036583102 scopus 로고    scopus 로고
    • Phototropins 1 and 2: Versatile plant blue-light receptors
    • W. R. Briggs J. M. Christie Phototropins 1 and 2: versatile plant blue-light receptors Trends Plant Sci. 2002 7 204-210.
    • (2002) Trends Plant Sci. , vol.7 , pp. 204-210
    • Briggs, W.R.1    Christie, J.M.2
  • 4
    • 14944349780 scopus 로고    scopus 로고
    • Plant blue-light receptors
    • R. Banerjee A. Batschauer Plant blue-light receptors Planta 2005 220 498-502.
    • (2005) Planta , vol.220 , pp. 498-502
    • Banerjee, R.1    Batschauer, A.2
  • 5
    • 0031470701 scopus 로고    scopus 로고
    • Arabidopsis NPH1: A Protein Kinase with a Putative Redox-Sensing Domain
    • E. Huala P. W. Oeller E. Liscum I. S. Han E. Larsen W. R. Briggs Arabidopsis NPH1: A Protein Kinase with a Putative Redox-Sensing Domain Science 1997 278 2120-2123.
    • (1997) Science , vol.278 , pp. 2120-2123
    • Huala, E.1    Oeller, P.W.2    Liscum, E.3    Han, I.S.4    Larsen, E.5    Briggs, W.R.6
  • 6
    • 14744270377 scopus 로고    scopus 로고
    • Autophosphorylation, electrophoretic mobility and immunoreaction of oat Phototropin 1 Under UV and Blue Light
    • E. Knieb M. Salomon W. Rüdiger Autophosphorylation, electrophoretic mobility and immunoreaction of oat Phototropin 1 Under UV and Blue Light Photochem. Photobiol. 2005 81 177-182.
    • (2005) Photochem. Photobiol. , vol.81 , pp. 177-182
    • Knieb, E.1    Salomon, M.2    Rüdiger, W.3
  • 7
    • 0034622586 scopus 로고    scopus 로고
    • Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor phototropin
    • M. Salomon J. M. Christie E. Knieb U. Lempert W. R. Briggs Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor phototropin Biochemistry 2000 39 9401-9410.
    • (2000) Biochemistry , vol.39 , pp. 9401-9410
    • Salomon, M.1    Christie, J.M.2    Knieb, E.3    Lempert, U.4    Briggs, W.R.5
  • 10
    • 0036016438 scopus 로고    scopus 로고
    • Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch
    • S. Crosson K. Moffat Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch Plant Cell 2002 14 1067-1075.
    • (2002) Plant Cell , vol.14 , pp. 1067-1075
    • Crosson, S.1    Moffat, K.2
  • 14
    • 0037306223 scopus 로고    scopus 로고
    • Phot-LOV1: Photocycle of a Blue-Light Receptor Domain from the Green Alga Chlamydomonas reinhardtii
    • T. Kottke J. Heberle Dominic Hehn P. Hegemann Phot-LOV1: Photocycle of a Blue-Light Receptor Domain from the Green Alga Chlamydomonas reinhardtii Biophys. J. 2003 84 1192-1201.
    • (2003) Biophys. J. , vol.84 , pp. 1192-1201
    • Kottke, T.1    Heberle Dominic Hehn, J.2    Hegemann, P.3
  • 15
    • 24944553332 scopus 로고    scopus 로고
    • Blue light-regulated molecular switch of Ser/Thr kinase in phototropin
    • D. Matsuoka S. Tokutomi Blue light-regulated molecular switch of Ser/Thr kinase in phototropin Proc. Natl. Acad. Sci. U. S. A. 2005 102 13337-13342.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 13337-13342
    • Matsuoka, D.1    Tokutomi, S.2
  • 16
    • 0036776294 scopus 로고    scopus 로고
    • Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function
    • J. M. Christie T. E. Swartz R. A. Bogomolni W. R. Briggs Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function Plant J. 2002 32 205-219.
    • (2002) Plant J. , vol.32 , pp. 205-219
    • Christie, J.M.1    Swartz, T.E.2    Bogomolni, R.A.3    Briggs, W.R.4
  • 17
    • 0037435618 scopus 로고    scopus 로고
    • The LOV domain family: Photoresponsive signaling modules coupled to diverse output domains
    • S. Crosson S. Rajagopal K. Moffat The LOV domain family: photoresponsive signaling modules coupled to diverse output domains Biochemistry 2003 42 2-10.
    • (2003) Biochemistry , vol.42 , pp. 2-10
    • Crosson, S.1    Rajagopal, S.2    Moffat, K.3
  • 18
    • 3242747589 scopus 로고    scopus 로고
    • The bacterial counterparts of plants phototropins
    • A. Losi The bacterial counterparts of plants phototropins Photochem. Photobiol. Sci. 2004 3 566-574.
    • (2004) Photochem. Photobiol. Sci. , vol.3 , pp. 566-574
    • Losi, A.1
  • 19
    • 0036224807 scopus 로고    scopus 로고
    • First evidence for phototropin-related blue-light receptors in prokaryotes
    • A. Losi E. Polverini B. Quest W. Gärtner First evidence for phototropin-related blue-light receptors in prokaryotes Biophys. J. 2002 82 2627-2634.
    • (2002) Biophys. J. , vol.82 , pp. 2627-2634
    • Losi, A.1    Polverini, E.2    Quest, B.3    Gärtner, W.4
  • 20
    • 19944390971 scopus 로고    scopus 로고
    • Initial characterization of a blue-light sensing, phototropin-related protein from Pseudomonas putida: A paradigm for an extended LOV construct
    • U. Krauss A. Losi W. Gärtner K.-E. Jaeger T. Eggert Initial characterization of a blue-light sensing, phototropin-related protein from Pseudomonas putida: a paradigm for an extended LOV construct Phys. Chem. Chem. Phys. 2005 7 2229-2236.
    • (2005) Phys. Chem. Chem. Phys. , vol.7 , pp. 2229-2236
    • Krauss, U.1    Losi, A.2    Gärtner, W.3    Jaeger, K.-E.4    Eggert, T.5
  • 22
    • 0035853139 scopus 로고    scopus 로고
    • Structure of a flavin-binding plant photoreceptor domain: Insights into light-mediated signal transduction
    • S. Crosson K. Moffat Structure of a flavin-binding plant photoreceptor domain: insights into light-mediated signal transduction Proc. Natl. Acad. Sci. U. S. A. 2001 98 2995-3000.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 2995-3000
    • Crosson, S.1    Moffat, K.2
  • 23
    • 0037380836 scopus 로고    scopus 로고
    • Crystal structures and molecular mechanism of a light-induced signaling switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii
    • R. Fedorov I. Schlichting E. Hartmann T. Domratcheva M. Fuhrmann P. Hegemann Crystal structures and molecular mechanism of a light-induced signaling switch: the Phot-LOV1 domain from Chlamydomonas reinhardtii Biophys. J. 2003 84 2492-2501.
    • (2003) Biophys. J. , vol.84 , pp. 2492-2501
    • Fedorov, R.1    Schlichting, I.2    Hartmann, E.3    Domratcheva, T.4    Fuhrmann, M.5    Hegemann, P.6
  • 24
    • 0141707094 scopus 로고    scopus 로고
    • Structural basis of a phototropin light switch
    • S. M. Harper L. C. Neil K. H. Gardner Structural basis of a phototropin light switch Science 2003 301 1541-1544.
    • (2003) Science , vol.301 , pp. 1541-1544
    • Harper, S.M.1    Neil, L.C.2    Gardner, K.H.3
  • 25
    • 11144344967 scopus 로고    scopus 로고
    • Disruption of the LOV-Jalpha helix interaction activates phototropin kinase activity
    • S. M. Harper J. M. Christie K. H. Gardner Disruption of the LOV-Jalpha helix interaction activates phototropin kinase activity Biochemistry 2004 43 16184-16192.
    • (2004) Biochemistry , vol.43 , pp. 16184-16192
    • Harper, S.M.1    Christie, J.M.2    Gardner, K.H.3
  • 26
    • 33745334847 scopus 로고    scopus 로고
    • D.-P. Häder and G. Jori, Elsevier, Amsterdam, 4th edn, ch. 10
    • A. Losi, in Flavin photochemistry and photobiology, ed. D.-P. Häder and G. Jori, Elsevier, Amsterdam, 4th edn, 2006, ch. 10, pp. 223–276.
    • (2006) Flavin Photochemistry and Photobiology , pp. 223-276
    • Losi, A.1
  • 27
    • 25444492902 scopus 로고    scopus 로고
    • Conformational dynamics of phototropin 2 LOV2 domain with the linker upon photoexcitation
    • T. Eitoku Y. Nakasone D. Matsuoka S. Tokutomi M. Terazima Conformational dynamics of phototropin 2 LOV2 domain with the linker upon photoexcitation J. Am. Chem. Soc. 2005 127 13238-13244.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 13238-13244
    • Eitoku, T.1    Nakasone, Y.2    Matsuoka, D.3    Tokutomi, S.4    Terazima, M.5
  • 28
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential and light
    • B. L. Taylor I. B. Zhulin PAS domains: internal sensors of oxygen, redox potential and light Microbiol. Mol. Biol. Rev. 1999 63 479-506.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 29
    • 10444268892 scopus 로고    scopus 로고
    • Heme-based sensors: Defining characteristics, recent developments, and regulatory hypotheses
    • M. A. Gilles-Gonzalez G. Gonzalez Heme-based sensors: defining characteristics, recent developments, and regulatory hypotheses J. Inorg. Biochem. 2005 99 1-22.
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 1-22
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2
  • 30
    • 4143081643 scopus 로고    scopus 로고
    • Dimerization of the plant photoreceptor phototropin is probably mediated by the LOV1 domain
    • M. Salomon U. Lempert W. Rüdiger Dimerization of the plant photoreceptor phototropin is probably mediated by the LOV1 domain FEBS Lett. 2004 572 8-10.
    • (2004) FEBS Lett. , vol.572 , pp. 8-10
    • Salomon, M.1    Lempert, U.2    Rüdiger, W.3
  • 31
    • 33745686031 scopus 로고    scopus 로고
    • Kinetic Measurement of Transient Dimerization and Dissociation Reactions of Arabidopsis Phototropin 1 LOV2 Domain
    • Y. Nakasone T. Eitoku D. Matsuoka S. Tokutomi M. Terazima Kinetic Measurement of Transient Dimerization and Dissociation Reactions of Arabidopsis Phototropin 1 LOV2 Domain Biophys. J. 2006 91 645-653.
    • (2006) Biophys. J. , vol.91 , pp. 645-653
    • Nakasone, Y.1    Eitoku, T.2    Matsuoka, D.3    Tokutomi, S.4    Terazima, M.5
  • 32
    • 13844261202 scopus 로고    scopus 로고
    • Quaternary structure of LOV-domain containing polypeptide of Arabidopsis FKF1 protein
    • M. Nakasako D. Matsuoka K. Zikihara S. Tokutomi Quaternary structure of LOV-domain containing polypeptide of Arabidopsis FKF1 protein FEBS Lett. 2005 579 1067-1071.
    • (2005) FEBS Lett. , vol.579 , pp. 1067-1071
    • Nakasako, M.1    Matsuoka, D.2    Zikihara, K.3    Tokutomi, S.4
  • 33
    • 9744263917 scopus 로고    scopus 로고
    • Light-Induced Structural Changes of LOV Domain-Containing Polypeptides from Arabidopsis Phototropin 1 and 2 Studied by Small-Angle X-ray Scattering
    • M. Nakasako T. Iwata D. Matsuoka S. Tokutomi Light-Induced Structural Changes of LOV Domain-Containing Polypeptides from Arabidopsis Phototropin 1 and 2 Studied by Small-Angle X-ray Scattering Biochemistry 2004 43 14881-1489.
    • (2004) Biochemistry , vol.43 , pp. 14881-21489
    • Nakasako, M.1    Iwata, T.2    Matsuoka, D.3    Tokutomi, S.4
  • 34
    • 0031880316 scopus 로고    scopus 로고
    • Roles in dimerization and blue light photoresponse of the PAS and LOV domains of Neurospora crassa white collar proteins
    • P. Ballario C. Talora D. Galli H. Linden G. Macino Roles in dimerization and blue light photoresponse of the PAS and LOV domains of Neurospora crassa white collar proteins Mol. Microbiol. 1998 29 719-729.
    • (1998) Mol. Microbiol. , vol.29 , pp. 719-729
    • Ballario, P.1    Talora, C.2    Galli, D.3    Linden, H.4    Macino, G.5
  • 35
    • 0033953284 scopus 로고    scopus 로고
    • The STAS domain a link between anion transporters and antisigma-factor antagonists
    • L. Aravind E. V. Koonin The STAS domain a link between anion transporters and antisigma-factor antagonists Curr. Biol. 2000 10 R53-R55.
    • (2000) Curr. Biol. , vol.10 , pp. R53-R55
    • Aravind, L.1    Koonin, E.V.2
  • 36
    • 0035141969 scopus 로고    scopus 로고
    • New family of regulators in the environmental signaling pathway which activates the general stress transcription factor of Bacillus subtilis
    • S. Akbar T. A. Gaidenko K. Min M. O’Reilly K. M. Devine C. W. Price New family of regulators in the environmental signaling pathway which activates the general stress transcription factor of Bacillus subtilis J. Bacteriol. 2001 183 1329-1338.
    • (2001) J. Bacteriol. , vol.183 , pp. 1329-1338
    • Akbar, S.1    Gaidenko, T.A.2    Min, K.3    O’Reilly, M.4    Devine, K.M.5    Price, C.W.6
  • 37
    • 33749014144 scopus 로고    scopus 로고
    • The blue-light receptor YtvA acts in the environmental stress signaling pathway of Bacillus subtilis
    • T. A. Gaidenko T. J. Kim A. L. Weigel M. S. Brody C. W. Price The blue-light receptor YtvA acts in the environmental stress signaling pathway of Bacillus subtilis J. Bacteriol. 2006 188 6387-6395.
    • (2006) J. Bacteriol. , vol.188 , pp. 6387-6395
    • Gaidenko, T.A.1    Kim, T.J.2    Weigel, A.L.3    Brody, M.S.4    Price, C.W.5
  • 38
    • 33749021097 scopus 로고    scopus 로고
    • Blue light activates the sigmaB-dependent stress response of Bacillus subtilisvia YtvA
    • M. Avila-Perez K. J. Hellingwerf R. Kort Blue light activates the sigmaB-dependent stress response of Bacillus subtilisvia YtvA J. Bacteriol. 2006 188 6411-6414.
    • (2006) J. Bacteriol. , vol.188 , pp. 6411-6414
    • Avila-Perez, M.1    Hellingwerf, K.J.2    Kort, R.3
  • 39
    • 33745404577 scopus 로고    scopus 로고
    • Blue news: NTP binding properties of the blue-light sensitive YtvA protein from Bacillus subtilis
    • V. Buttani A. Losi E. Polverini W. Gärtner Blue news: NTP binding properties of the blue-light sensitive YtvA protein from Bacillus subtilis FEBS Lett. 2006 580 3818-3822.
    • (2006) FEBS Lett. , vol.580 , pp. 3818-3822
    • Buttani, V.1    Losi, A.2    Polverini, E.3    Gärtner, W.4
  • 40
    • 0029904582 scopus 로고    scopus 로고
    • The SpoIIAA protein of Bacillus subtilis has GTP-binding properties
    • S. M. Najafi D. A. Harris M. D. Yudkin The SpoIIAA protein of Bacillus subtilis has GTP-binding properties J. Bacteriol. 1996 178 6632-6634.
    • (1996) J. Bacteriol. , vol.178 , pp. 6632-6634
    • Najafi, S.M.1    Harris, D.A.2    Yudkin, M.D.3
  • 41
    • 27544498857 scopus 로고    scopus 로고
    • Mutational effects on protein structural changes and interdomain interactions in the blue-light sensing LOV protein YtvA
    • A. Losi E. Ghiraldelli S. Jansen W. Gärtner Mutational effects on protein structural changes and interdomain interactions in the blue-light sensing LOV protein YtvA Photochem. Photobiol. 2005 81 1145-1152.
    • (2005) Photochem. Photobiol. , vol.81 , pp. 1145-1152
    • Losi, A.1    Ghiraldelli, E.2    Jansen, S.3    Gärtner, W.4
  • 42
    • 1142304289 scopus 로고    scopus 로고
    • Listening to the blue: The time-resolved thermodynamics of the bacterial blue-light receptor YtvA and its isolated LOV domain
    • A. Losi B. Quest W. Gärtner Listening to the blue: the time-resolved thermodynamics of the bacterial blue-light receptor YtvA and its isolated LOV domain Photochem. Photobiol. Sci. 2003 2 759-766.
    • (2003) Photochem. Photobiol. Sci. , vol.2 , pp. 759-766
    • Losi, A.1    Quest, B.2    Gärtner, W.3
  • 43
    • 0025861478 scopus 로고
    • Convex constraint analysis: A natural deconvolution of circular dichroism curves of proteins
    • A. Perczel M. Hollosi G. Tusnady G. D. Fasman Convex constraint analysis: a natural deconvolution of circular dichroism curves of proteins Protein Eng. 1991 4 669-679.
    • (1991) Protein Eng. , vol.4 , pp. 669-679
    • Perczel, A.1    Hollosi, M.2    Tusnady, G.3    Fasman, G.D.4
  • 44
    • 0026696116 scopus 로고
    • Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: A practical guide
    • A. Perczel K. Park G. D. Fasman Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: A practical guide Anal. Biochem. 1992 203 83-93.
    • (1992) Anal. Biochem. , vol.203 , pp. 83-93
    • Perczel, A.1    Park, K.2    Fasman, G.D.3
  • 47
    • 0345832301 scopus 로고    scopus 로고
    • ClusPro: An automated docking and discrimination method for the prediction of protein complexes
    • S. R. Comeau D. W. Gatchell S. Vajda C. J. Camacho ClusPro: An automated docking and discrimination method for the prediction of protein complexes Bioinformatics 2004 20 45-50.
    • (2004) Bioinformatics , vol.20 , pp. 45-50
    • Comeau, S.R.1    Gatchell, D.W.2    Vajda, S.3    Camacho, C.J.4
  • 49
    • 0038526303 scopus 로고    scopus 로고
    • ZDOCK: An initial-stage protein-docking algorithm
    • R. Chen L. Li Z. Weng ZDOCK: an initial-stage protein-docking algorithm Proteins 2003 52 80-87.
    • (2003) Proteins , vol.52 , pp. 80-87
    • Chen, R.1    Li, L.2    Weng, Z.3
  • 53
    • 0027180507 scopus 로고
    • Verification of protein structures: Patterns of nonbonded atomic interactions
    • C. Colovos T. O. Yeates Verification of protein structures: patterns of nonbonded atomic interactions Protein Sci. 1993 2 1511-1519.
    • (1993) Protein Sci. , vol.2 , pp. 1511-1519
    • Colovos, C.1    Yeates, T.O.2
  • 54
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • R. Luthy J. U. Bowie D. Eisenberg Assessment of protein models with three-dimensional profiles Nature 1992 356 83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 55
    • 0030598343 scopus 로고    scopus 로고
    • Deviations from standard atomic volumes as a quality measure for protein crystal structures
    • J. Pontius J. Richelle S. J. Wodak Deviations from standard atomic volumes as a quality measure for protein crystal structures J. Mol. Biol. 1996 264 121-136.
    • (1996) J. Mol. Biol. , vol.264 , pp. 121-136
    • Pontius, J.1    Richelle, J.2    Wodak, S.J.3
  • 56
    • 17444372787 scopus 로고    scopus 로고
    • Improved prediction of protein-protein binding sites using a support vector machines approach
    • J. R. Bradford D. R. Westhead Improved prediction of protein-protein binding sites using a support vector machines approach Bioinformatics 2005 21 1487-1494.
    • (2005) Bioinformatics , vol.21 , pp. 1487-1494
    • Bradford, J.R.1    Westhead, D.R.2
  • 57
    • 3242879771 scopus 로고    scopus 로고
    • Computational alanine scanning of protein–protein interfaces
    • T. Kortemme D. E. Kim D. Baker Computational alanine scanning of protein–protein interfaces Sci. STKE 2004 2004 219 pls2.
    • (2004) Sci. STKE , vol.2004 , Issue.219 , pp. pls2
    • Kortemme, T.1    Kim, D.E.2    Baker, D.3
  • 58
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Inclusion of denatured proteins with native proteins in the analysis
    • N. Sreerama S. Y. Venyaminov R. W. Woody Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis Anal. Biochem. 2000 287 243-251.
    • (2000) Anal. Biochem. , vol.287 , pp. 243-251
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 59
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy
    • N. Sreerama S. Y. Venyaminov R. W. Woody Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy Protein Sci. 1999 8 370-380.
    • (1999) Protein Sci. , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 60
    • 23344444462 scopus 로고    scopus 로고
    • Improved Estimation of the Secondary Structures of Proteins by Vacuum-Ultraviolet Circular Dichroism Spectroscopy
    • K. Matsuo R. Yonehara K. Gekko Improved Estimation of the Secondary Structures of Proteins by Vacuum-Ultraviolet Circular Dichroism Spectroscopy J. Biochem. 2005 138 79-88.
    • (2005) J. Biochem. , vol.138 , pp. 79-88
    • Matsuo, K.1    Yonehara, R.2    Gekko, K.3
  • 61
    • 0037302324 scopus 로고    scopus 로고
    • Structural composition of betaI- and betaII-proteins
    • N. Sreerama R. W. Woody Structural composition of betaI- and betaII-proteins Protein Sci. 2003 12 384-388.
    • (2003) Protein Sci. , vol.12 , pp. 384-388
    • Sreerama, N.1    Woody, R.W.2
  • 62
    • 1642486696 scopus 로고    scopus 로고
    • Analysis of circular dichroism data
    • N. J. Greenfield Analysis of circular dichroism data Methods Enzymol. 2004 383 282-317.
    • (2004) Methods Enzymol. , vol.383 , pp. 282-317
    • Greenfield, N.J.1
  • 63
    • 0037058903 scopus 로고    scopus 로고
    • Recent developments in the electronic spectroscopy of amides and alpha-helical polypeptides
    • R. W. Woody A. Koslowski Recent developments in the electronic spectroscopy of amides and alpha-helical polypeptides Biophys. Chem. 2002 101–102 535-551.
    • (2002) Biophys. Chem. , vol.101-102 , pp. 535-551
    • Woody, R.W.1    Koslowski, A.2
  • 64
    • 0030042763 scopus 로고    scopus 로고
    • Methods to estimate the conformation of proteins and polypeptides from circular dichroism data
    • N. J. Greenfield Methods to estimate the conformation of proteins and polypeptides from circular dichroism data Anal. Biochem. 1996 235 1-10.
    • (1996) Anal. Biochem. , vol.235 , pp. 1-10
    • Greenfield, N.J.1
  • 65
    • 0018118041 scopus 로고
    • Circular dichroic analysis of protein conformation: Inclusion of the beta-turns
    • C. T. Chang C. S. Wu J. T. Yang Circular dichroic analysis of protein conformation: inclusion of the beta-turns Anal. Biochem. 1978 91 13-31.
    • (1978) Anal. Biochem. , vol.91 , pp. 13-31
    • Chang, C.T.1    Wu, C.S.2    Yang, J.T.3
  • 66
    • 18844391283 scopus 로고    scopus 로고
    • Comparative investigation of the LOV1 and LOV2 domains in Adiantum Phytochrome3
    • T. Iwata D. Nozaki S. Tokutomi H. Kandori Comparative investigation of the LOV1 and LOV2 domains in Adiantum Phytochrome3 Biochemistry 2005 44 7427-7434.
    • (2005) Biochemistry , vol.44 , pp. 7427-7434
    • Iwata, T.1    Nozaki, D.2    Tokutomi, S.3    Kandori, H.4
  • 67
    • 0037428497 scopus 로고    scopus 로고
    • Intramolecular proton transfers and structural changes during the photocycle of the LOV2 domain of phototropin 1
    • S. B. Corchnoy T. E. Swartz J. W. Lewis I. Szundi W. R. Briggs R. A. Bogomolni Intramolecular proton transfers and structural changes during the photocycle of the LOV2 domain of phototropin 1 J. Biol. Chem. 2003 278 724-731.
    • (2003) J. Biol. Chem. , vol.278 , pp. 724-731
    • Corchnoy, S.B.1    Swartz, T.E.2    Lewis, J.W.3    Szundi, I.4    Briggs, W.R.5    Bogomolni, R.A.6
  • 69
    • 26244466162 scopus 로고    scopus 로고
    • Structural Basis of ARNT PAS-B dimerization: Use of a common beta-sheet interface for hetero- and homodimerization
    • P. B. Card P. J. A. Erbel K. H. Gardner Structural Basis of ARNT PAS-B dimerization: use of a common beta-sheet interface for hetero- and homodimerization J. Mol. Biol. 2005 353 664-677.
    • (2005) J. Mol. Biol. , vol.353 , pp. 664-677
    • Card, P.B.1    Erbel, P.J.A.2    Gardner, K.H.3
  • 70
    • 1542327658 scopus 로고    scopus 로고
    • Insights into signal transduction involving PAS domain oxygen-sensing heme proteins from the X-ray crystal structure of Escherichia Coli Dos Heme Domain (EcDosH)
    • H. J. Park C. Suquet J. D. Satterlee C. Kang Insights into signal transduction involving PAS domain oxygen-sensing heme proteins from the X-ray crystal structure of Escherichia Coli Dos Heme Domain (EcDosH) Biochemistry 2004 43 2738-2746.
    • (2004) Biochemistry , vol.43 , pp. 2738-2746
    • Park, H.J.1    Suquet, C.2    Satterlee, J.D.3    Kang, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.