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Volumn 132, Issue 4, 2002, Pages 591-595

Biophysical effect of amino acids on the prevention of protein aggregation

Author keywords

Amino acid; Dilution induced aggregation from denaturant; Heat induced aggregation; Protein aggregation

Indexed keywords

AMINO ACID; PROTEIN; ARGININE;

EID: 0036774673     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a003261     Document Type: Article
Times cited : (249)

References (16)
  • 1
    • 0025671869 scopus 로고
    • Refolding and aggregation of bovine carbonic anhydrase B: Quasi-elastic light scattering analysis
    • Cleland, J.L. and Wang, D.I.C. (1990) Refolding and aggregation of bovine carbonic anhydrase B: Quasi-elastic light scattering analysis. Biochemistry 29, 11072-11078
    • (1990) Biochemistry , vol.29 , pp. 11072-11078
    • Cleland, J.L.1    Wang, D.I.C.2
  • 2
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • Fink, A.L. (1998) Protein aggregation: Folding aggregates, inclusion bodies and amyloid. Fold. Design 3, R9-R23
    • (1998) Fold. Design. , vol.3 , pp. R9-R23
    • Fink, A.L.1
  • 5
    • 0018788361 scopus 로고
    • Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation
    • Zettlmeissl, G., Rudolph, R., and Jaenicke, R. (1979) Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation. Biochemistry 18, 5567-5571
    • (1979) Biochemistry , vol.18 , pp. 5567-5571
    • Zettlmeissl, G.1    Rudolph, R.2    Jaenicke, R.3
  • 6
    • 0020435643 scopus 로고
    • Nonspecific stabilization of stress-susceptible proteins by stress-resistant proteins: A model for the biological role of heat shock proteins
    • Minton, K.W., Karman, P., Hahn, G.M., and Minton, A.P. (1982) Nonspecific stabilization of stress-susceptible proteins by stress-resistant proteins: A model for the biological role of heat shock proteins. Proc. Natl. Acad. Sci. USA 79, 7107-7111
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 7107-7111
    • Minton, K.W.1    Karman, P.2    Hahn, G.M.3    Minton, A.P.4
  • 7
    • 0026734937 scopus 로고
    • Rationalization of the effects of compatible solutes on protein stability in terras of thermodynamic nonideality
    • Winzor, C.L., Winzor, D.J., Paleg, L.G., Jones, G.P., and Naidu, B.P. (1992) Rationalization of the effects of compatible solutes on protein stability in terras of thermodynamic nonideality. Arch. Biochem. Biophys. 296, 102-107
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 102-107
    • Winzor, C.L.1    Winzor, D.J.2    Paleg, L.G.3    Jones, G.P.4    Naidu, B.P.5
  • 8
    • 0028559525 scopus 로고
    • Folding and aggregation of TEM beta-lactamase: Analogies with the formation of inclusion bodies in Escherichia coli
    • Georgiou, G., Valax, P., Ostermeier, M., and Horowitz, P.M. (1994) Folding and aggregation of TEM beta-lactamase: Analogies with the formation of inclusion bodies in Escherichia coli. Protein Sci. 3, 1953-1960
    • (1994) Protein Sci. , vol.3 , pp. 1953-1960
    • Georgiou, G.1    Valax, P.2    Ostermeier, M.3    Horowitz, P.M.4
  • 10
    • 0026510381 scopus 로고
    • Independent domain folding of Pseudomonas exotoxin and single-chain immunotoxins: Influence of interdomain connections
    • Brinkmann, U., Buchner, J., and Pastan, I. (1992) Independent domain folding of Pseudomonas exotoxin and single-chain immunotoxins: Influence of interdomain connections. Proc. Natl. Acad. Sci. USA 89, 3075-3079
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3075-3079
    • Brinkmann, U.1    Buchner, J.2    Pastan, I.3
  • 11
    • 0006454079 scopus 로고
    • Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli
    • Buchner, J. and Rudolph, R. (1991) Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli. Biotechnology 9, 157-162
    • (1991) Biotechnology , vol.9 , pp. 157-162
    • Buchner, J.1    Rudolph, R.2
  • 12
    • 0027978242 scopus 로고
    • Increased thermal stability of proteins in the presence of amino acids
    • Taneja, S. and Ahmad, F. (1994) Increased thermal stability of proteins in the presence of amino acids. Biochem. J. 303, 147-153
    • (1994) Biochem. J. , vol.303 , pp. 147-153
    • Taneja, S.1    Ahmad, F.2
  • 13
    • 0035021006 scopus 로고    scopus 로고
    • Role of proline, glycerol, and heparin as protein folding aids during refolding of rabbit muscle creatine kinase
    • Meng, F., Park, Y., and Zhou, H. (2001) Role of proline, glycerol, and heparin as protein folding aids during refolding of rabbit muscle creatine kinase. Int. J. Biochem. Cell Biol. 33, 701-709
    • (2001) Int. J. Biochem. Cell Biol. , vol.33 , pp. 701-709
    • Meng, F.1    Park, Y.2    Zhou, H.3
  • 14
    • 0028978422 scopus 로고
    • Trifluoroethanol-induced stabilization of the alpha-helical structure of beta-lactoglobulin: Implication for non-hierarchical protein folding
    • Shiraki, K., Nishikawa, K., and Goto, Y. (1995) Trifluoroethanol-induced stabilization of the alpha-helical structure of beta-lactoglobulin: implication for non-hierarchical protein folding. J. Mol. Biol. 245, 180-194
    • (1995) J. Mol. Biol. , vol.245 , pp. 180-194
    • Shiraki, K.1    Nishikawa, K.2    Goto, Y.3
  • 15
    • 0030046574 scopus 로고    scopus 로고
    • In vitro folding of inclusion body proteins
    • Rudolph, R. and Lilie, H. (1996) In vitro folding of inclusion body proteins. FASEB J. 10, R49-R56
    • (1996) FASEB J. , vol.10 , pp. R49-R56
    • Rudolph, R.1    Lilie, H.2
  • 16
    • 0030712099 scopus 로고    scopus 로고
    • Co-refolding denatured-reduced hen egg white lysozyme with acidic and basic proteins
    • Trivedi, V.D., Raman, B., Rao, C.M., and Ramakrishna, T. (1997) Co-refolding denatured-reduced hen egg white lysozyme with acidic and basic proteins. FEBS Lett. 418, 363-366
    • (1997) FEBS Lett. , vol.418 , pp. 363-366
    • Trivedi, V.D.1    Raman, B.2    Rao, C.M.3    Ramakrishna, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.