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Volumn 352, Issue 2, 2006, Pages 299-301

A nondetergent sulfobetaine prevents protein aggregation in microcalorimetric studies

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY;

EID: 33646151145     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2006.01.035     Document Type: Article
Times cited : (23)

References (15)
  • 3
    • 0032901515 scopus 로고    scopus 로고
    • Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition
    • Jelesarov I., and Bosshard H.R. Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition. J. Mol. Recognit. 12 (1999) 3-18
    • (1999) J. Mol. Recognit. , vol.12 , pp. 3-18
    • Jelesarov, I.1    Bosshard, H.R.2
  • 4
    • 0037197677 scopus 로고    scopus 로고
    • Maximal stabilities of reversible two-state proteins
    • Kumar S., Tsai C.J., and Nussinov R. Maximal stabilities of reversible two-state proteins. Biochemistry 41 (2002) 5359-5374
    • (2002) Biochemistry , vol.41 , pp. 5359-5374
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 5
    • 0035854688 scopus 로고    scopus 로고
    • Structural determinants of cold adaptation and stability in a large protein
    • D'Amico S., Gerday C., and Feller G. Structural determinants of cold adaptation and stability in a large protein. J. Biol. Chem. 276 (2001) 25791-25796
    • (2001) J. Biol. Chem. , vol.276 , pp. 25791-25796
    • D'Amico, S.1    Gerday, C.2    Feller, G.3
  • 6
    • 0037424370 scopus 로고    scopus 로고
    • Activity-stability relationships in extremophilic enzymes
    • D'Amico S., Marx J.C., Gerday C., and Feller G. Activity-stability relationships in extremophilic enzymes. J. Biol. Chem. 278 (2003) 7891-7896
    • (2003) J. Biol. Chem. , vol.278 , pp. 7891-7896
    • D'Amico, S.1    Marx, J.C.2    Gerday, C.3    Feller, G.4
  • 7
    • 0037466287 scopus 로고    scopus 로고
    • Activity, stability and flexibility in glycosidases adapted to extreme thermal environments
    • Collins T., Meuwis M.A., Gerday C., and Feller G. Activity, stability and flexibility in glycosidases adapted to extreme thermal environments. J. Mol. Biol. 328 (2003) 419-428
    • (2003) J. Mol. Biol. , vol.328 , pp. 419-428
    • Collins, T.1    Meuwis, M.A.2    Gerday, C.3    Feller, G.4
  • 8
    • 0141596172 scopus 로고    scopus 로고
    • Structural and functional adaptations to extreme temperatures in psychrophilic, mesophilic, and thermophilic DNA ligases
    • Georlette D., Damien B., Blaise V., Depiereux E., Uversky V.N., Gerday C., and Feller G. Structural and functional adaptations to extreme temperatures in psychrophilic, mesophilic, and thermophilic DNA ligases. J. Biol. Chem. 278 (2003) 37015-37023
    • (2003) J. Biol. Chem. , vol.278 , pp. 37015-37023
    • Georlette, D.1    Damien, B.2    Blaise, V.3    Depiereux, E.4    Uversky, V.N.5    Gerday, C.6    Feller, G.7
  • 9
    • 1842509102 scopus 로고    scopus 로고
    • Psychrophilic enzymes: hot topics in cold adaptation
    • Feller G., and Gerday C. Psychrophilic enzymes: hot topics in cold adaptation. Nat. Rev. Microbiol. 1 (2003) 200-208
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 200-208
    • Feller, G.1    Gerday, C.2
  • 10
    • 0033528657 scopus 로고    scopus 로고
    • Thermodynamic stability of a cold-active alpha-amylase from the Antarctic bacterium Alteromonas haloplanctis
    • Feller G., d'Amico D., and Gerday C. Thermodynamic stability of a cold-active alpha-amylase from the Antarctic bacterium Alteromonas haloplanctis. Biochemistry 38 (1999) 4613-4619
    • (1999) Biochemistry , vol.38 , pp. 4613-4619
    • Feller, G.1    d'Amico, D.2    Gerday, C.3
  • 11
    • 2942560270 scopus 로고    scopus 로고
    • Purification, characterization, and sequencing of an extracellular cold-active aminopeptidase produced by marine psychrophile Colwellia psychrerythraea strain 34H
    • Huston A.L., Methe B., and Deming J.W. Purification, characterization, and sequencing of an extracellular cold-active aminopeptidase produced by marine psychrophile Colwellia psychrerythraea strain 34H. Appl. Environ. Microbiol. 70 (2004) 3321-3328
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 3321-3328
    • Huston, A.L.1    Methe, B.2    Deming, J.W.3
  • 12
    • 29244485572 scopus 로고    scopus 로고
    • Stability domains, substrate-induced conformational changes and hinge-bending motions in a psychrophilic phosphoglycerate kinase: a microcalorimetric study
    • Zecchinon L., Oriol A., Netzel U., Svennberg J., Gerardin-Otthiers N., and Feller G. Stability domains, substrate-induced conformational changes and hinge-bending motions in a psychrophilic phosphoglycerate kinase: a microcalorimetric study. J. Biol. Chem. 280 (2005) 41307-41314
    • (2005) J. Biol. Chem. , vol.280 , pp. 41307-41314
    • Zecchinon, L.1    Oriol, A.2    Netzel, U.3    Svennberg, J.4    Gerardin-Otthiers, N.5    Feller, G.6
  • 13
    • 0028797534 scopus 로고
    • Non-detergent sulphobetaines: a new class of mild solubilization agents for protein purification
    • Vuillard L., Braun-Breton C., and Rabilloud T. Non-detergent sulphobetaines: a new class of mild solubilization agents for protein purification. Biochem. J. 305 (1995) 337-343
    • (1995) Biochem. J. , vol.305 , pp. 337-343
    • Vuillard, L.1    Braun-Breton, C.2    Rabilloud, T.3
  • 14
    • 0032529064 scopus 로고    scopus 로고
    • Interactions of non-detergent sulfobetaines with early folding intermediates facilitate in vitro protein renaturation
    • Vuillard L., Rabilloud T., and Goldberg M.E. Interactions of non-detergent sulfobetaines with early folding intermediates facilitate in vitro protein renaturation. Eur. J. Biochem. 256 (1998) 128-135
    • (1998) Eur. J. Biochem. , vol.256 , pp. 128-135
    • Vuillard, L.1    Rabilloud, T.2    Goldberg, M.E.3
  • 15
    • 20444493910 scopus 로고    scopus 로고
    • Scan-rate-dependent melting transitions of interleukin-1 receptor (type II): elucidation of meaningful thermodynamic and kinetic parameters of aggregation acquired from DSC simulations
    • Remmele Jr. R.L., Zhang-van Enk J., Dharmavaram V., Balaban D., Durst M., Shoshitaishvili A., and Rand H. Scan-rate-dependent melting transitions of interleukin-1 receptor (type II): elucidation of meaningful thermodynamic and kinetic parameters of aggregation acquired from DSC simulations. J. Am. Chem. Soc. 127 (2005) 8328-8339
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 8328-8339
    • Remmele Jr., R.L.1    Zhang-van Enk, J.2    Dharmavaram, V.3    Balaban, D.4    Durst, M.5    Shoshitaishvili, A.6    Rand, H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.