메뉴 건너뛰기




Volumn 1008, Issue , 2013, Pages 211-241

Circular and linear dichroism spectroscopy for the study of protein-ligand interactions

Author keywords

Chirality; Circular dichroism; Induced circular dichroism; Ligand binding; Linear dichroism; Proteins

Indexed keywords

HUMAN SERUM ALBUMIN; LIGAND; AMINO ACID; PROTEIN; PROTEIN BINDING; PROTEIN SUBUNIT;

EID: 84925558650     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-62703-398-5_8     Document Type: Article
Times cited : (19)

References (30)
  • 4
    • 84883187850 scopus 로고    scopus 로고
    • http://dichroweb.cryst.bbk.ac.uk;. CDsstr byW. Curtis Johnson
    • http://dichroweb.cryst.bbk.ac.uk; Dichroweb by Lee Whitmore and B.A. Wallace http://oregonstate. edu/dept/biochem/faculty/johnson. html. CDsstr byW. Curtis Johnson
    • Dichroweb by Lee Whitmore and B.A Wallace
  • 5
    • 0033562629 scopus 로고    scopus 로고
    • Analyzing protein circular dichroism spectra for accurate secondary structures
    • Johnson WC (1999) Analyzing protein circular dichroism spectra for accurate secondary structures. Proteins 35:307-312
    • (1999) Proteins , vol.35 , pp. 307-312
    • Johnson, W.C.1
  • 6
    • 28844477180 scopus 로고    scopus 로고
    • Validation of new microvolume Couette flow linear dichroism cells
    • Marrington R, Dafforn TR, Halsall DJ, Hicks M, Rodger A (2005) Validation of new microvolume Couette flow linear dichroism cells. Analyst 130:1608-1616
    • (2005) Analyst , vol.130 , pp. 1608-1616
    • Marrington, R.1    Dafforn, T.R.2    Halsall, D.J.3    Hicks, M.4    Rodger, A.5
  • 7
    • 4444261853 scopus 로고    scopus 로고
    • Micro volume Couette flow sample orientation for absorbance and fluorescence linear dichroism
    • Marrington R, Dafforn TR, Halsall DJ, 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
  • 9
    • 52949116417 scopus 로고    scopus 로고
    • Folding and membrane insertion of the pore-forming peptide gramicidin occur as a concerted process
    • Hicks MR, Damianoglou A, Rodger A, Dafforn TR (2008) Folding and membrane insertion of the pore-forming peptide gramicidin occur as a concerted process. J Mol Biol 383:358-366
    • (2008) J Mol Biol , vol.383 , pp. 358-366
    • Hicks, M.R.1    Damianoglou, A.2    Rodger, A.3    Dafforn, T.R.4
  • 10
    • 77955777573 scopus 로고    scopus 로고
    • LD spectroscopy of natural and synthetic biomaterials
    • Hicks MR, Kowalski J, Rodger A (2010) LD spectroscopy of natural and synthetic biomaterials. Chem Soc Rev 39:3380-3393
    • (2010) Chem Soc Rev , vol.39 , pp. 3380-3393
    • Hicks, M.R.1    Kowalski, J.2    Rodger, A.3
  • 11
    • 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, 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
  • 12
    • 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 TR, Addinall S (2004) FtsZ fibre bundling is triggered by a calcium-induced conformational change in bound GTP. J Biol Chem 279:48821-48829
    • (2004) J Biol Chem , vol.279 , pp. 48821-48829
    • Marrington, R.1    Small, E.2    Rodger, A.3    Dafforn, T.R.4    Addinall, S.5
  • 13
    • 0000367088 scopus 로고
    • Two-point calibration of circular dichrometer with d-10-camphorsulfonic acid
    • Chen GC, Yang JT (1977) Two-point calibration of circular dichrometer with d-10-camphorsulfonic acid. Anal Lett 10:1195-1207
    • (1977) Anal Lett , vol.10 , pp. 1195-1207
    • Chen, G.C.1    Yang, J.T.2
  • 14
    • 84998283298 scopus 로고
    • A new standard substance for calibration of circular dichroism: Ammonium d-10-camphorsulfonate
    • Takakuwa T, Konno T, Meguro H (1985) A new standard substance for calibration of circular dichroism: Ammonium d-10-camphorsulfonate. Anal Sci 1:215-218
    • (1985) Anal Sci , vol.1 , pp. 215-218
    • Takakuwa, T.1    Konno, T.2    Meguro, H.3
  • 16
    • 84865656086 scopus 로고    scopus 로고
    • Considerations of noise and measurement reproducibility of cd measurements using na[coiii (edds
    • Chmel NP, Scott P, Rodger A (2012) Considerations of noise and measurement reproducibility of CD measurements using Na[CoIII (EDDS)]. Chirality 24:699-705
    • (2012) Chirality , vol.24 , pp. 699-705
    • Chmel, N.P.1    Scott, P.2    Rodger, A.3
  • 17
    • 70349314208 scopus 로고    scopus 로고
    • Synchrotron radiation linear dichroism spectroscopy of the antibiotic peptide gramicidin in lipid membranes
    • Hicks MR, Dafforn TR, Damianoglou A, Wormell P, Rodger A, Hoffmann SV (2009) Synchrotron radiation linear dichroism spectroscopy of the antibiotic peptide gramicidin in lipid membranes. Analyst 134:1623-1628
    • (2009) Analyst , vol.134 , pp. 1623-1628
    • Hicks, M.R.1    Dafforn, T.R.2    Damianoglou, A.3    Wormell, P.4    Rodger, A.5    Hoffmann, S.V.6
  • 18
    • 0027431453 scopus 로고
    • Linear dichroism
    • Rodger A (1993) Linear dichroism. Methods Enzymol 226:232-258
    • (1993) Methods Enzymol , vol.226 , pp. 232-258
    • Rodger, A.1
  • 21
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace CN (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 131:266-280
    • (1986) Methods Enzymol , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 22
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC, von Hippel PH (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182:319-326
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 23
    • 0348147599 scopus 로고    scopus 로고
    • Calibration and standardisation of synchrotron radiation circular dichroism and conventional circular dichroism spectrophotometers
    • Miles AJ, Wien F, Lees JG, Rodger A, Janes RW, Wallace BA (2003) Calibration and standardisation of synchrotron radiation circular dichroism and conventional circular dichroism spectrophotometers. Spectroscopy 17:653-661
    • (2003) Spectroscopy , vol.17 , pp. 653-661
    • Miles, A.J.1    Wien, F.2    Lees, J.G.3    Rodger, A.4    Janes, R.W.5    Wallace, B.A.6
  • 26
    • 0023785593 scopus 로고
    • Secondary structure of proteins through circular dichroism spectroscopy
    • Johnson WCJ (1988) Secondary structure of proteins through circular dichroism spectroscopy. Annu Rev Biophys Biophys Chem 17:145-166
    • (1988) Annu Rev Biophys Biophys Chem , vol.17 , pp. 145-166
    • Johnson, W.C.J.1
  • 27
    • 0021944965 scopus 로고
    • Circular dichroism and its empirical application to biopolymers
    • Johnson WCJ (1985) Circular dichroism and its empirical application to biopolymers. Methods Biochem Anal 31:61-163
    • (1985) Methods Biochem Anal , vol.31 , pp. 61-163
    • Johnson, W.C.J.1
  • 28
    • 0042928465 scopus 로고    scopus 로고
    • An Escherichia coli twin-Arginine signal peptide switches between helical and unstructured conformations depending on hydrophobicity of the environment
    • Miguel MS, Marrington R, Rodger PM, Rodger A, Robinson C (2003) An Escherichia coli twin-Arginine signal peptide switches between helical and unstructured conformations depending on hydrophobicity of the environment. Eur J Biochem 270:3345-3352
    • (2003) Eur J Biochem , vol.270 , pp. 3345-3352
    • Miguel, M.S.1    Marrington, R.2    Rodger, P.M.3    Rodger, A.4    Robinson, C.5
  • 29
    • 84883183035 scopus 로고    scopus 로고
    • In Chemistry, University of Warwick, Coventry
    • Green P (1999) PhD thesis, In Chemistry, University of Warwick, Coventry
    • (1999) PhD Thesis
    • Green, P.1
  • 30
    • 78649798863 scopus 로고    scopus 로고
    • The synergistic action of melittin and phospholipase A2 with lipid membranes: Development of linear dichroism for membrane-insertion kinetics
    • DamianoglouA, Rodger A, PridmoreC, Dafforn TR, Mosely JA, Sanderson JM, HicksMR(2010) The synergistic action of melittin and phospholipase A2 with lipid membranes: Development of linear dichroism for membrane-insertion kinetics. Protein Pept Lett 17:1351-1362
    • (2010) Protein Pept Lett , vol.17 , pp. 1351-1362
    • Damianoglou, A.1    Rodger, A.2    Pridmore, C.3    Dafforn, T.R.4    Mosely, J.A.5    Sanderson, J.M.6    Hicks, M.R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.