메뉴 건너뛰기




Volumn 91, Issue 4, 2008, Pages 377-396

How to study DNA and proteins by linear dichroism spectroscopy

Author keywords

DNA; Linear dichroism; Proteins

Indexed keywords


EID: 58149489298     PISSN: 00368504     EISSN: None     Source Type: Journal    
DOI: 10.3184/003685008X395517     Document Type: Article
Times cited : (8)

References (31)
  • 1
    • 4544276100 scopus 로고    scopus 로고
    • Flow linear dichroism to probe binding of aromatic molecules and DNA to single walled carbon nanotubes
    • Rajendra, J., Baxendale, M., Dit Rap, L.G. and Rodger, A. (2004) Flow linear dichroism to probe binding of aromatic molecules and DNA to single walled carbon nanotubes. J. Am. Chem. Soc., 126, 11182-11188.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 11182-11188
    • Rajendra, J.1    Baxendale, M.2    Dit Rap, L.G.3    Rodger, A.4
  • 2
    • 23744499214 scopus 로고    scopus 로고
    • The binding of single stranded DNA and PNA to single walled carbon nanotubes probed by flow linear dichroism
    • Rajendra, J. and Rodger, A. (2005) The binding of single stranded DNA and PNA to single walled carbon nanotubes probed by flow linear dichroism. Chem. Eur J., 11, 4841-4848.
    • (2005) Chem. Eur J , vol.11 , pp. 4841-4848
    • Rajendra, J.1    Rodger, A.2
  • 3
    • 4444261853 scopus 로고    scopus 로고
    • Micro volume Couette flow sample orientation for absorbance and fluorescence linear dichroism
    • Marrington, R., Dafforn, T.R., Halsall, D.J. and Rodger, A. (2004) Micro volume Couette flow sample orientation for absorbance and fluorescence linear dichroism. Biophys. J., 87, 2002-2012.
    • (2004) Biophys. J , vol.87 , pp. 2002-2012
    • Marrington, R.1    Dafforn, T.R.2    Halsall, D.J.3    Rodger, A.4
  • 19
    • 55349142832 scopus 로고    scopus 로고
    • DNA binding and bending by dinuclear complexes comprising ruthenium polypyridyl centres linked by a bis(pyridylimine) ligand
    • McDonnell, U., Hicks, M.R., Hannon, MJ and Rodger, A. (2008) DNA binding and bending by dinuclear complexes comprising ruthenium polypyridyl centres linked by a bis(pyridylimine) ligand. J. Inorg. Biochem., 102, 2052-2059.
    • (2008) J. Inorg. Biochem , vol.102 , pp. 2052-2059
    • McDonnell, U.1    Hicks, M.R.2    Hannon, M.J.3    Rodger, A.4
  • 20
    • 17044403057 scopus 로고    scopus 로고
    • Type II restriction endonucleases: Structure and mechanism
    • Pingoud, A., Fuxreiter, M., Pingoud, V and Wende, W. (2005) Type II restriction endonucleases: structure and mechanism. Cell. Mol. Life Sci., 62, 685-707.
    • (2005) Cell. Mol. Life Sci , vol.62 , pp. 685-707
    • Pingoud, A.1    Fuxreiter, M.2    Pingoud, V.3    Wende, W.4
  • 22
    • 0032539688 scopus 로고    scopus 로고
    • Real-time enzyme kinetics monitored by dual-color fluorescence cross-correlation spectroscopy
    • Kettling, U, Koltermann, A., Schwille, P. and Eigen, M. (1998) Real-time enzyme kinetics monitored by dual-color fluorescence cross-correlation spectroscopy. Proc. Natl. Acad. Sci. USA, 95, 1416-20.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1416-1420
    • Kettling, U.1    Koltermann, A.2    Schwille, P.3    Eigen, M.4
  • 23
    • 0026627728 scopus 로고
    • Continuous spectrophotometric assay for restriction endonucleases using synthetic oligodeoxynucleotides and based on the hyperchromic effect
    • Waters, T.R. and Connolly, B.A. (1992) Continuous spectrophotometric assay for restriction endonucleases using synthetic oligodeoxynucleotides and based on the hyperchromic effect. Analyt. Biochem., 204, 204-209.
    • (1992) Analyt. Biochem , vol.204 , pp. 204-209
    • Waters, T.R.1    Connolly, B.A.2
  • 24
    • 10344248919 scopus 로고    scopus 로고
    • FtsZ fibre bundling is triggered by a calcium-induced conformational change in bound GTP
    • Marrington, R., Small, E., Rodger, A., Dafforn, T.R. and Addinall, S.G. (2004) FtsZ fibre bundling is triggered by a calcium-induced conformational change in bound GTP. J. Biol. Chem., 47, 48821-48829.
    • (2004) J. Biol. Chem , vol.47 , pp. 48821-48829
    • Marrington, R.1    Small, E.2    Rodger, A.3    Dafforn, T.R.4    Addinall, S.G.5
  • 25
    • 34247495145 scopus 로고    scopus 로고
    • FtsZ polymer-bundling by the Escherichia coli ZapA orthologue, YgfE involves a conformational change in bound GTP
    • Small, E., Marrington, R., Rodger, A., Scott, D.J., Sloan. K., Roper, D., Dafforn, T.R. and Addinall, S.G. (2007) FtsZ polymer-bundling by the Escherichia coli ZapA orthologue, YgfE involves a conformational change in bound GTP. J Mol. Biol., 369, 211-221.
    • (2007) J Mol. Biol , vol.369 , pp. 211-221
    • Small, E.1    Marrington, R.2    Rodger, A.3    Scott, D.J.4    Sloan, K.5    Roper, D.6    Dafforn, T.R.7    Addinall, S.G.8
  • 26
    • 33748801723 scopus 로고    scopus 로고
    • A new method for fibrous protein analysis illustrated by application to tubulin microtubule polymerisation and depolymerisation
    • Marrington, R., Seymour, M. and Rodger, A. (2006) A new method for fibrous protein analysis illustrated by application to tubulin microtubule polymerisation and depolymerisation. Chirality, 18, 680-690.
    • (2006) Chirality , vol.18 , pp. 680-690
    • Marrington, R.1    Seymour, M.2    Rodger, A.3
  • 27
    • 0024471771 scopus 로고
    • Orientation of the bases of single-stranded DNA and polynucleotides in complexes formed with the gene 32 protein of bacteriophage T4. A linear dichroism study
    • van Amerongen, H. and van Grondelle, R. (1989) Orientation of the bases of single-stranded DNA and polynucleotides in complexes formed with the gene 32 protein of bacteriophage T4. A linear dichroism study. J. Mol. Biol., 209, 433-445..
    • (1989) J. Mol. Biol , vol.209 , pp. 433-445
    • van Amerongen, H.1    van Grondelle, R.2
  • 28
    • 0032582070 scopus 로고    scopus 로고
    • Chromophore Orientation in Liposome Membranes Probed with Flow Linear Dichroism
    • Ardhammar, M., Mikati, N. and Nordén, B. (1998) Chromophore Orientation in Liposome Membranes Probed with Flow Linear Dichroism. J. Am. Chem. Soc., 120, 9957-9958.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 9957-9958
    • Ardhammar, M.1    Mikati, N.2    Nordén, B.3
  • 30
    • 0015244581 scopus 로고
    • Rhodospin-like protein from the purple membrane of Halobacterium halobium
    • Oesterhelt, D. and Stoeckenius, W. (1971) Rhodospin-like protein from the purple membrane of Halobacterium halobium. Nature New Biol., 233, 149-152.
    • (1971) Nature New Biol , vol.233 , pp. 149-152
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 31
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson, R., Baldwin, J.M., Ceska, T.A., Zemlin, F., Beckmann, E. and Downing, K.H. (1990) Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol., 213, 899-929.
    • (1990) J. Mol. Biol , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.