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Volumn 114, Issue 2-3, 2005, Pages 205-212

Temperature effect on the structural stability, similarity, and reversibility of human serum albumin in different states

Author keywords

FTIR; HAS; Structural similarity; Thermal reversibility; Thermal stability

Indexed keywords

HUMAN SERUM ALBUMIN; HYDROGEN;

EID: 17144392510     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2004.12.004     Document Type: Article
Times cited : (34)

References (34)
  • 1
    • 0003527686 scopus 로고    scopus 로고
    • Protein structure, stability, and folding
    • Humana Press Totowa, NJ, USA
    • K.P. Murphy Protein structure, stability, and folding Methods in Molecular Biology vol. 168 2001 Humana Press Totowa, NJ, USA
    • (2001) Methods in Molecular Biology , vol.168
    • Murphy, K.P.1
  • 3
    • 0030059689 scopus 로고    scopus 로고
    • Forces contributing to the conformational stability of proteins
    • C.N. Pace, B.A. Shirley, M. McNutt, and K. Gajiwala Forces contributing to the conformational stability of proteins FASEB J. 10 1996 75 83
    • (1996) FASEB J. , vol.10 , pp. 75-83
    • Pace, C.N.1    Shirley, B.A.2    McNutt, M.3    Gajiwala, K.4
  • 4
    • 0000159569 scopus 로고    scopus 로고
    • Protein structure and the energetics of protein stability
    • A.D. Robertson, and K.P. Murphy Protein structure and the energetics of protein stability Chem. Rev. 97 1997 1251 1268
    • (1997) Chem. Rev. , vol.97 , pp. 1251-1268
    • Robertson, A.D.1    Murphy, K.P.2
  • 5
    • 0030834850 scopus 로고    scopus 로고
    • Temperature, stability, and the hydrophobic interaction
    • J.A. Schellman Temperature, stability, and the hydrophobic interaction Biophys. J. 73 1997 2960 2964
    • (1997) Biophys. J. , vol.73 , pp. 2960-2964
    • Schellman, J.A.1
  • 7
    • 0036599564 scopus 로고    scopus 로고
    • Practical aspects of the ligand-binding and enzymatic properties of human serum albumin
    • U. Kragh-Hansen, V.T. Chuang, and M. Otagiri Practical aspects of the ligand-binding and enzymatic properties of human serum albumin Biol. Pharm. Bull. 25 2002 695 704
    • (2002) Biol. Pharm. Bull. , vol.25 , pp. 695-704
    • Kragh-Hansen, U.1    Chuang, V.T.2    Otagiri, M.3
  • 8
    • 2342588126 scopus 로고    scopus 로고
    • Multiple-probe analysis of folding and unfolding pathways of human serum albumin. Evidence for a framework mechanism of folding
    • M.K. Santra, A. Banerjee, S.S. Krishnakumar, O. Rahaman, and D. Panda Multiple-probe analysis of folding and unfolding pathways of human serum albumin. Evidence for a framework mechanism of folding Eur. J. Biochem. 271 2004 1789 1797
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1789-1797
    • Santra, M.K.1    Banerjee, A.2    Krishnakumar, S.S.3    Rahaman, O.4    Panda, D.5
  • 10
  • 11
    • 0035992779 scopus 로고    scopus 로고
    • Reversible and covalent binding of drugs to human serum albumin: Methodological approaches and physiological relevance
    • C. Bertucci, and E. Domenici Reversible and covalent binding of drugs to human serum albumin: methodological approaches and physiological relevance Curr. Med. Chem. 9 2002 1463 1481
    • (2002) Curr. Med. Chem. , vol.9 , pp. 1463-1481
    • Bertucci, C.1    Domenici, E.2
  • 12
    • 1842839884 scopus 로고    scopus 로고
    • Effect of ethanol or/and captopril on the secondary structure of human serum albumin before and after protein binding
    • S.Y. Lin, Y.S. Wei, M.J. Li, and S.L. Wang Effect of ethanol or/and captopril on the secondary structure of human serum albumin before and after protein binding Eur. J. Pharm. Biopharm. 57 2004 457 464
    • (2004) Eur. J. Pharm. Biopharm. , vol.57 , pp. 457-464
    • Lin, S.Y.1    Wei, Y.S.2    Li, M.J.3    Wang, S.L.4
  • 13
    • 5444269342 scopus 로고    scopus 로고
    • Ethanol or/and captopril-induced precipitation and secondary conformational changes of human serum albumin
    • S.Y. Lin, Y.S. Wei, and M.J. Li Ethanol or/and captopril-induced precipitation and secondary conformational changes of human serum albumin Spectrochim. Acta, Part A: Mol. Biomol. Spectrosc. 60 2004 3107 3111
    • (2004) Spectrochim. Acta, Part A: Mol. Biomol. Spectrosc. , vol.60 , pp. 3107-3111
    • Lin, S.Y.1    Wei, Y.S.2    Li, M.J.3
  • 14
    • 0037422474 scopus 로고    scopus 로고
    • Subtractive similarity method used to study the infrared spectra of proteins in aqueous solution
    • S.L. Wang, Y.S. Wei, and S.Y. Lin Subtractive similarity method used to study the infrared spectra of proteins in aqueous solution Vibr. Spectrosc. 31 2003 313 319
    • (2003) Vibr. Spectrosc. , vol.31 , pp. 313-319
    • Wang, S.L.1    Wei, Y.S.2    Lin, S.Y.3
  • 15
    • 0000843080 scopus 로고    scopus 로고
    • Applications of infrared spectroscopy to medical biology
    • P. Franck, P. Nabet, and B. Dousset Applications of infrared spectroscopy to medical biology Cell. Mol. Biol. 44 1998 273 275
    • (1998) Cell. Mol. Biol. , vol.44 , pp. 273-275
    • Franck, P.1    Nabet, P.2    Dousset, B.3
  • 16
    • 0033564112 scopus 로고    scopus 로고
    • Infrared spectroscopy
    • L.M. Ng, and R. Simmons Infrared spectroscopy Anal. Chem. 71 1999 343R 350R
    • (1999) Anal. Chem. , vol.71
    • Ng, L.M.1    Simmons, R.2
  • 17
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • M. Jackson, and H.H. Mantsch The use and misuse of FTIR spectroscopy in the determination of protein structure Crit. Rev. Biochem. Mol. Biol. 30 1995 95 120
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 18
    • 0029438076 scopus 로고
    • Fourier transform infrared spectroscopy investigations of protein structure
    • E.A. Cooper, and K. Knutson Fourier transform infrared spectroscopy investigations of protein structure Pharm. Biotechnol. 7 1995 101 143
    • (1995) Pharm. Biotechnol. , vol.7 , pp. 101-143
    • Cooper, E.A.1    Knutson, K.2
  • 19
    • 0023377695 scopus 로고
    • Thermal denaturation of globular proteins. Fourier transform-infrared studies of the amide III spectral region
    • G. Anderle, and R. Mendelsohn Thermal denaturation of globular proteins. Fourier transform-infrared studies of the amide III spectral region Biophys. J. 52 1987 69 74
    • (1987) Biophys. J. , vol.52 , pp. 69-74
    • Anderle, G.1    Mendelsohn, R.2
  • 20
    • 1542357647 scopus 로고    scopus 로고
    • A distinct utility of the amide III infrared band for secondary structure estimation of aqueous protein solutions using partial least squares methods
    • S. Cai, and B.R. Singh A distinct utility of the amide III infrared band for secondary structure estimation of aqueous protein solutions using partial least squares methods Biochemistry 43 2004 2541 2549
    • (2004) Biochemistry , vol.43 , pp. 2541-2549
    • Cai, S.1    Singh, B.R.2
  • 21
    • 0348107343 scopus 로고    scopus 로고
    • In vitro simulation of solid-solid dehydration, rehydration, and solidification of trehalose dihydrate using thermal and vibrational spectroscopic techniques
    • S.Y. Lin, and J.L. Chien In vitro simulation of solid-solid dehydration, rehydration, and solidification of trehalose dihydrate using thermal and vibrational spectroscopic techniques Pharm. Res. 20 2003 1926 1931
    • (2003) Pharm. Res. , vol.20 , pp. 1926-1931
    • Lin, S.Y.1    Chien, J.L.2
  • 22
    • 0041886417 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy used to evidence the prevention of beta-sheet formation of amyloid beta(1-40) peptide by a short amyloid fragment
    • S.Y. Lin, and H.L. Chu Fourier transform infrared spectroscopy used to evidence the prevention of beta-sheet formation of amyloid beta(1-40) peptide by a short amyloid fragment Int. J. Biol. Macromol. 32 2003 173 177
    • (2003) Int. J. Biol. Macromol. , vol.32 , pp. 173-177
    • Lin, S.Y.1    Chu, H.L.2
  • 23
    • 0027176042 scopus 로고
    • Separation of freezing- and drying-induced denaturation of lyophilized proteins using stress-specific stabilization. II: Structural studies using infrared spectroscopy
    • S.J. Prestrelski, T. Arakawa, and J.F. Carpenter Separation of freezing- and drying-induced denaturation of lyophilized proteins using stress-specific stabilization. II: Structural studies using infrared spectroscopy Arch. Biochem. Biophys. 303 1993 465 473
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 465-473
    • Prestrelski, S.J.1    Arakawa, T.2    Carpenter, J.F.3
  • 24
    • 0029002812 scopus 로고
    • The conformational analysis of peptides using Fourier transform IR spectroscopy
    • P.I. Haris, and D. Chapman The conformational analysis of peptides using Fourier transform IR spectroscopy Biopolymers 37 1995 251 263
    • (1995) Biopolymers , vol.37 , pp. 251-263
    • Haris, P.I.1    Chapman, D.2
  • 25
    • 0028847040 scopus 로고
    • Lyophilization-induced reversible changes in the secondary structure of proteins
    • K. Griebenow, and A.M. Klibanov Lyophilization-induced reversible changes in the secondary structure of proteins Proc. Natl. Acad. Sci. U. S. A. 92 1995 10969 10976
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 10969-10976
    • Griebenow, K.1    Klibanov, A.M.2
  • 26
    • 0141457919 scopus 로고    scopus 로고
    • Studies on the interaction of total saponins of panax notoginseng and human serum albumin by Fourier transform infrared spectroscopy
    • Y. Liu, M.X. Xie, J. Kang, and D. Zheng Studies on the interaction of total saponins of panax notoginseng and human serum albumin by Fourier transform infrared spectroscopy Spectrochim. Acta, Part A: Mol. Biomol. Spectrosc. 59 2003 2747 2758
    • (2003) Spectrochim. Acta, Part A: Mol. Biomol. Spectrosc. , vol.59 , pp. 2747-2758
    • Liu, Y.1    Xie, M.X.2    Kang, J.3    Zheng, D.4
  • 27
    • 0030152443 scopus 로고    scopus 로고
    • Determination of the secondary structure of isomeric forms of human serum albumin by a particular frequency deconvolution procedure applied to Fourier transform IR analysis
    • E. Bramanti, and E. Benedetti Determination of the secondary structure of isomeric forms of human serum albumin by a particular frequency deconvolution procedure applied to Fourier transform IR analysis Biopolymers 38 1996 639 653
    • (1996) Biopolymers , vol.38 , pp. 639-653
    • Bramanti, E.1    Benedetti, E.2
  • 28
    • 0032560039 scopus 로고    scopus 로고
    • Interaction of cisplatin with human serum albumin. Drug binding mode and protein secondary structure
    • J.F. Neault, and H.A. Tajmir-Riahi Interaction of cisplatin with human serum albumin. Drug binding mode and protein secondary structure Biochim. Biophys. Acta 1384 1998 153 159
    • (1998) Biochim. Biophys. Acta , vol.1384 , pp. 153-159
    • Neault, J.F.1    Tajmir-Riahi, H.A.2
  • 29
    • 0035887070 scopus 로고    scopus 로고
    • Fourier transform infrared spectrometric analysis of protein conformation: Effect of sampling method and stress factors
    • M. van de Weert, P.I. Haris, W.E. Hennink, and D.J. Crommelin Fourier transform infrared spectrometric analysis of protein conformation: effect of sampling method and stress factors Anal. Biochem. 297 2001 160 169
    • (2001) Anal. Biochem. , vol.297 , pp. 160-169
    • Van De Weert, M.1    Haris, P.I.2    Hennink, W.E.3    Crommelin, D.J.4
  • 30
    • 0035842073 scopus 로고    scopus 로고
    • Fourier-transform infrared spectroscopic study of globulin from Phaseolus angularis (red bean)
    • G.T. Meng, and C.Y. Ma Fourier-transform infrared spectroscopic study of globulin from Phaseolus angularis (red bean) Int. J. Biol. Macromol. 29 2001 287 294
    • (2001) Int. J. Biol. Macromol. , vol.29 , pp. 287-294
    • Meng, G.T.1    Ma, C.Y.2
  • 31
    • 0034331056 scopus 로고    scopus 로고
    • Biopharmaceutical powders: Particle formation and formulation considerations
    • Y.F. Maa, and S.J. Prestrelski Biopharmaceutical powders: particle formation and formulation considerations Curr. Pharm. Biotechnol. 1 2000 283 302
    • (2000) Curr. Pharm. Biotechnol. , vol.1 , pp. 283-302
    • Maa, Y.F.1    Prestrelski, S.J.2
  • 32
    • 0033975702 scopus 로고    scopus 로고
    • Structural energetics of protein folding and binding
    • S.P. Edgcomb, and K.P. Murphy Structural energetics of protein folding and binding Curr. Opin. Biotechnol. 11 2000 62 66
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 62-66
    • Edgcomb, S.P.1    Murphy, K.P.2
  • 33
    • 0037007468 scopus 로고    scopus 로고
    • Protein stability: The value of 'old literature'
    • F. Franks Protein stability: the value of 'old literature' Biophys. Chem. 96 2002 117 127
    • (2002) Biophys. Chem. , vol.96 , pp. 117-127
    • Franks, F.1


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