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Volumn 11, Issue 2, 2006, Pages 131-137

DMSO-related effects in protein characterization

Author keywords

Biophysical characterization; DMSO; DMSO effects; Protein aggregation; Protein stability

Indexed keywords

DIMETHYL SULFOXIDE; GROWTH HORMONE RECEPTOR; HUMAN GROWTH HORMONE; PHOSPHATASE;

EID: 33644938893     PISSN: 10870571     EISSN: 1552454X     Source Type: Journal    
DOI: 10.1177/1087057105284218     Document Type: Article
Times cited : (136)

References (21)
  • 3
    • 0028099433 scopus 로고
    • Structural stability of lipase from wheat germ
    • Rajeshwara AN, Prakash V: Structural stability of lipase from wheat germ. Int J Pept Protein Res 1994;44:435-440.
    • (1994) Int J Pept Protein Res , vol.44 , pp. 435-440
    • Rajeshwara, A.N.1    Prakash, V.2
  • 4
    • 0028931842 scopus 로고
    • Mechanism of solvent-induced thermal stabilization of alpha-amylase from Bacillus amyloliquefaciens
    • Rajendran S, Radha C, Prakash V: Mechanism of solvent-induced thermal stabilization of alpha-amylase from Bacillus amyloliquefaciens. Int J Pept Protein Res 1995;45:122-128.
    • (1995) Int J Pept Protein Res , vol.45 , pp. 122-128
    • Rajendran, S.1    Radha, C.2    Prakash, V.3
  • 5
    • 0030701981 scopus 로고    scopus 로고
    • Effects of organic solvents on protein structures: Observation of a structured helical core in hen egg-white lysozyme in aqueous dimethylsulfoxide
    • Bhattacharjya S, Balaram P: Effects of organic solvents on protein structures: observation of a structured helical core in hen egg-white lysozyme in aqueous dimethylsulfoxide. Proteins: Structure, Function and Genetic 1997;29:492-507.
    • (1997) Proteins: Structure, Function and Genetic , vol.29 , pp. 492-507
    • Bhattacharjya, S.1    Balaram, P.2
  • 6
    • 0019327092 scopus 로고
    • Specific solvent effects on the thermal denaturation of ribonuclease: Effect of dimethyl sulfoxide and p-dioxane on thermodynamics of denaturation
    • Jacobson AL, Turner CL: Specific solvent effects on the thermal denaturation of ribonuclease: effect of dimethyl sulfoxide and p-dioxane on thermodynamics of denaturation. Biochemistry 1980;19:4534-4538.
    • (1980) Biochemistry , vol.19 , pp. 4534-4538
    • Jacobson, A.L.1    Turner, C.L.2
  • 7
    • 0020010452 scopus 로고
    • Effect of dimethylsulfoxide and its homologues on the thermal denaturation of lysozyme as measured by differential scanning calorimetry
    • Fujita Y, Izumiguchi S, Noda Y: Effect of dimethylsulfoxide and its homologues on the thermal denaturation of lysozyme as measured by differential scanning calorimetry. Int J Pept Protein Res 1982;19:25-31.
    • (1982) Int J Pept Protein Res , vol.19 , pp. 25-31
    • Fujita, Y.1    Izumiguchi, S.2    Noda, Y.3
  • 8
    • 0030835825 scopus 로고    scopus 로고
    • Preferential solvation changes upon lysozyme heat denaturation in mixed solvents
    • Kovrigin EL, Potekhin SA: Preferential solvation changes upon lysozyme heat denaturation in mixed solvents. Biochemistry 1997;36:9195-9199.
    • (1997) Biochemistry , vol.36 , pp. 9195-9199
    • Kovrigin, E.L.1    Potekhin, S.A.2
  • 9
    • 0014422825 scopus 로고
    • Dimethyl sulfoxide: An inhibitor of liver alcohol dehydrogenase
    • Perlman RL, Wolff J: Dimethyl sulfoxide: an inhibitor of liver alcohol dehydrogenase. Science 1968;160:317-319.
    • (1968) Science , vol.160 , pp. 317-319
    • Perlman, R.L.1    Wolff, J.2
  • 10
    • 0034604256 scopus 로고    scopus 로고
    • Spectroscopic studies of inhibited alcohol dehydrogenase from Thermoanaerobacter brockii: Proposed structure for the catalytic intermediate state
    • Kleifeld O, Frenkel A, Bogin O, Eisenstein M, Brumfeld V, Burstein Y, et al: Spectroscopic studies of inhibited alcohol dehydrogenase from Thermoanaerobacter brockii: proposed structure for the catalytic intermediate state. Biochemistry 2000;39:7702-7711.
    • (2000) Biochemistry , vol.39 , pp. 7702-7711
    • Kleifeld, O.1    Frenkel, A.2    Bogin, O.3    Eisenstein, M.4    Brumfeld, V.5    Burstein, Y.6
  • 11
    • 0344720263 scopus 로고    scopus 로고
    • Dimethyl sulfoxide binding to globular proteins: A nuclear magnetic relaxation dispersion study
    • Jóhannesson H, Denisov VP, Halle B : Dimethyl sulfoxide binding to globular proteins: a nuclear magnetic relaxation dispersion study. Protein Sci 1997;6:1756-1763.
    • (1997) Protein Sci , vol.6 , pp. 1756-1763
    • Jóhannesson, H.1    Denisov, V.P.2    Halle, B.3
  • 12
    • 33644934493 scopus 로고
    • Enzyme-catalyzed reactions
    • Jacob SW, Rosenbaum EE, Wood DC (eds): New York: Marcel Dekker
    • Rammler DH: Enzyme-catalyzed reactions. In Jacob SW, Rosenbaum EE, Wood DC (eds): Dimethyl Sulfoxide (Basic Concepts). New York: Marcel Dekker, 1971.
    • (1971) Dimethyl Sulfoxide (Basic Concepts)
    • Rammler, D.H.1
  • 13
    • 1342310505 scopus 로고    scopus 로고
    • Dimethyl sulfoxide at 2.5% (v/v) alters the structural cooperativity and unfolding mechanism of dimeric bacterial NAD+ synthetase
    • Yang ZW, Tendian SW, Carson WM, Brouillette WJ, Delucas LJ, Brouillette CG: Dimethyl sulfoxide at 2.5% (v/v) alters the structural cooperativity and unfolding mechanism of dimeric bacterial NAD+ synthetase. Protein Sci 2004;13:830-841.
    • (2004) Protein Sci , vol.13 , pp. 830-841
    • Yang, Z.W.1    Tendian, S.W.2    Carson, W.M.3    Brouillette, W.J.4    Delucas, L.J.5    Brouillette, C.G.6
  • 14
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck P: Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys J 2000;78:1606-1619.
    • (2000) Biophys J , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 15
    • 0025674590 scopus 로고
    • Probing conformational changes in proteins by mass spectrometry
    • Chowdhury SK, Katta V, Chait BT: Probing conformational changes in proteins by mass spectrometry. J Am Chem Soc 1990;112:9012-9013.
    • (1990) J Am Chem Soc , vol.112 , pp. 9012-9013
    • Chowdhury, S.K.1    Katta, V.2    Chait, B.T.3
  • 16
    • 0036182699 scopus 로고    scopus 로고
    • Uncoupled analysis of secondary and tertiary protein structure by circular dichroism and electrospray ionization mass spectrometry
    • Grandori R, Matecko I, Muller N: Uncoupled analysis of secondary and tertiary protein structure by circular dichroism and electrospray ionization mass spectrometry. J Mass Spectrom 2001;37:191-196.
    • (2001) J Mass Spectrom , vol.37 , pp. 191-196
    • Grandori, R.1    Matecko, I.2    Muller, N.3
  • 17
    • 0036388229 scopus 로고    scopus 로고
    • Detection of a receptor-ligand non-covalent complex using a triple quadrupole mass spectrometer
    • Lengqvist J, Griffiths WJ, Perlmann T, Sjövall J: Detection of a receptor-ligand non-covalent complex using a triple quadrupole mass spectrometer. Rapid Commun Mass Spectrom 2002;16:2003-2006.
    • (2002) Rapid Commun Mass Spectrom , vol.16 , pp. 2003-2006
    • Lengqvist, J.1    Griffiths, W.J.2    Perlmann, T.3    Sjövall, J.4
  • 18
    • 3543008337 scopus 로고    scopus 로고
    • Determination of dissociation constants for protein-ligand complexes by electrospray ionization mass spectrometry
    • Tjernberg A, Carnö S, Oliv F, Benkestock K, Edlund P-O, Griffiths WJ, et al: Determination of dissociation constants for protein-ligand complexes by electrospray ionization mass spectrometry. Anal Chem 2004;76:4325-4331.
    • (2004) Anal Chem , vol.76 , pp. 4325-4331
    • Tjernberg, A.1    Carnö, S.2    Oliv, F.3    Benkestock, K.4    Edlund, P.-O.5    Griffiths, W.J.6
  • 19
    • 4744344760 scopus 로고    scopus 로고
    • Features of the ESI mechanism that affect the observation of multiply charged noncovalent protein complexes and the determination of the association constant by the titration method
    • Peschke M, Verkerk UH, Kebarle P: Features of the ESI mechanism that affect the observation of multiply charged noncovalent protein complexes and the determination of the association constant by the titration method. J Am Soc Mass Spectrom 2004;15:1424-1434.
    • (2004) J Am Soc Mass Spectrom , vol.15 , pp. 1424-1434
    • Peschke, M.1    Verkerk, U.H.2    Kebarle, P.3
  • 20
    • 0018786675 scopus 로고
    • Structural differences between apo- and holoenzyme of horse liver alcohol dehydrogenase
    • Eklund H, Brändén C: Structural differences between apo- and holoenzyme of horse liver alcohol dehydrogenase. J Biol Chem 1979;254:3458-3461.
    • (1979) J Biol Chem , vol.254 , pp. 3458-3461
    • Eklund, H.1    Brändén, C.2
  • 21
    • 0020965337 scopus 로고
    • Inhibition by carboxamides and sulfoxides of liver alcohol dehydrogenase and ethanol metabolism
    • Chadha VK, Leidal KG, Plapp BV: Inhibition by carboxamides and sulfoxides of liver alcohol dehydrogenase and ethanol metabolism. J Med Chem 1983;26:916-922.
    • (1983) J Med Chem , vol.26 , pp. 916-922
    • Chadha, V.K.1    Leidal, K.G.2    Plapp, B.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.