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Volumn 61, Issue 2, 2011, Pages 313-325

Structural Stability as a Probe for Molecular Evolution of Homologous Albumins Studied by Spectroscopy and Bioinformatics

Author keywords

Chemical denaturant; Circular dichroism; Fluorescence spectroscopy; Free energy; Molecular evolution; Molecular modeling

Indexed keywords

GUANIDINE; SERUM ALBUMIN; UREA;

EID: 80955158812     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12013-011-9214-4     Document Type: Article
Times cited : (33)

References (53)
  • 2
    • 0034602966 scopus 로고    scopus 로고
    • Five recombinant fragments of human serum albumin-tools for the characterization of the warfarin binding site
    • Dockal, M., Carter, D. C., & Ruker, F. (2000). Five recombinant fragments of human serum albumin-tools for the characterization of the warfarin binding site. J Biol Chem, 275, 3042-3050.
    • (2000) J Biol Chem , vol.275 , pp. 3042-3050
    • Dockal, M.1    Carter, D.C.2    Ruker, F.3
  • 3
    • 0034237709 scopus 로고    scopus 로고
    • Anion-induced stabilization of human serum albumin prevents the formation of intermediate during urea denaturation
    • Muzammil, S., Kumar, Y., & Tayyab, S. (2000). Anion-induced stabilization of human serum albumin prevents the formation of intermediate during urea denaturation. Proteins, 40, 29-38.
    • (2000) Proteins , vol.40 , pp. 29-38
    • Muzammil, S.1    Kumar, Y.2    Tayyab, S.3
  • 4
    • 0023388641 scopus 로고
    • Urea-induced structural transformations in bovine serum albumin
    • Khan, M. Y., Agarwal, S. K., & Hangloo, S. (1987). Urea-induced structural transformations in bovine serum albumin. Journal of Biochemistry, 102, 313-317.
    • (1987) Journal of Biochemistry , vol.102 , pp. 313-317
    • Khan, M.Y.1    Agarwal, S.K.2    Hangloo, S.3
  • 5
    • 46849091776 scopus 로고    scopus 로고
    • Bromophenol blue binding as a probe to study urea and guanidine hydrochloride denaturation of bovine serum albumin
    • Halim, A. A. A., Kadir, H. A., & Tayyab, S. (2008). Bromophenol blue binding as a probe to study urea and guanidine hydrochloride denaturation of bovine serum albumin. Journal of Biochemistry, 144, 33-38.
    • (2008) Journal of Biochemistry , vol.144 , pp. 33-38
    • Halim, A.A.A.1    Kadir, H.A.2    Tayyab, S.3
  • 6
    • 0031901772 scopus 로고    scopus 로고
    • Species differences of serum albumins: III. Analysis of structural characteristics and ligand binding properties during N-B transitions
    • Kosa, T., Maruyama, T., Sakai, N., Yonemura, N., Yahara, S., & Otagiri, M. (1998). Species differences of serum albumins: III. Analysis of structural characteristics and ligand binding properties during N-B transitions. Pharmaceutical Research, 15, 592-598.
    • (1998) Pharmaceutical Research , vol.15 , pp. 592-598
    • Kosa, T.1    Maruyama, T.2    Sakai, N.3    Yonemura, N.4    Yahara, S.5    Otagiri, M.6
  • 7
    • 58849083625 scopus 로고    scopus 로고
    • How methyl cyanide induces aggregation in all-alpha proteins: A case study in four albumins
    • Sen, P., Fatima, S., Khan, J. M., & Khan, R. H. (2009). How methyl cyanide induces aggregation in all-alpha proteins: A case study in four albumins. International Journal of Biological Macromolecules, 44, 163-169.
    • (2009) International Journal of Biological Macromolecules , vol.44 , pp. 163-169
    • Sen, P.1    Fatima, S.2    Khan, J.M.3    Khan, R.H.4
  • 8
    • 70349923640 scopus 로고    scopus 로고
    • Interaction of Bovine (BSA), Rabbit (RSA), and Porcine (PSA) serum albumins with cationic single-chain/gemini surfactants: A comparative study
    • Gull, N., Sen, P., Khan, R. H., & Kabir-Ud-Din, (2009). Interaction of Bovine (BSA), Rabbit (RSA), and Porcine (PSA) serum albumins with cationic single-chain/gemini surfactants: A comparative study. Langmuir, 25, 11686-11691.
    • (2009) Langmuir , vol.25 , pp. 11686-11691
    • Gull, N.1    Sen, P.2    Khan, R.H.3    Kabir-Ud-Din4
  • 9
    • 36849088039 scopus 로고    scopus 로고
    • The minimal structural requirement of concanavalin A that retains its functional aspects
    • Ahmad, E., Naeem, A., Javed, S., Yadav, S., & Khan, R. H. (2007). The minimal structural requirement of concanavalin A that retains its functional aspects. Journal of Biochemistry, 142, 307-315.
    • (2007) Journal of Biochemistry , vol.142 , pp. 307-315
    • Ahmad, E.1    Naeem, A.2    Javed, S.3    Yadav, S.4    Khan, R.H.5
  • 10
    • 0034685617 scopus 로고    scopus 로고
    • Local and long-range interactions in the molten globule state: A study of chimeric proteins of bovine and human alpha-lactalbumin
    • Mizuguchi, M., Masaki, K., Demura, M., & Nitta, K. (2000). Local and long-range interactions in the molten globule state: A study of chimeric proteins of bovine and human alpha-lactalbumin. Journal of Molecular Biology, 298, 985-995.
    • (2000) Journal of Molecular Biology , vol.298 , pp. 985-995
    • Mizuguchi, M.1    Masaki, K.2    Demura, M.3    Nitta, K.4
  • 12
    • 23244452958 scopus 로고    scopus 로고
    • Effect of urea on peptide conformation in water: Molecular dynamics and experimental characterization
    • Caballero-Herrera, A., Nordstrand, K., Berndt, K. D., & Nilsson, L. (2005). Effect of urea on peptide conformation in water: Molecular dynamics and experimental characterization. Biophysical Journal, 89, 842-857.
    • (2005) Biophysical Journal , vol.89 , pp. 842-857
    • Caballero-Herrera, A.1    Nordstrand, K.2    Berndt, K.D.3    Nilsson, L.4
  • 13
    • 33750186642 scopus 로고    scopus 로고
    • The influence of urea on the structure of proteins in reversed micelles
    • Caetano, W., Amaral, C. L., & Itri, R. (2006). The influence of urea on the structure of proteins in reversed micelles. J Nanosci Nanotechnol, 6, 2416-2424.
    • (2006) J Nanosci Nanotechnol , vol.6 , pp. 2416-2424
    • Caetano, W.1    Amaral, C.L.2    Itri, R.3
  • 14
    • 0034649231 scopus 로고    scopus 로고
    • Use of domain specific ligands to study urea-induced unfolding of bovine serum albumin
    • Tayyab, S., Sharma, N., & Khan, M. M. (2000). Use of domain specific ligands to study urea-induced unfolding of bovine serum albumin. Biochemical and Biophysical Research Communications, 277, 83-88.
    • (2000) Biochemical and Biophysical Research Communications , vol.277 , pp. 83-88
    • Tayyab, S.1    Sharma, N.2    Khan, M.M.3
  • 15
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., & von Hippel, P. H. (1989). Calculation of protein extinction coefficients from amino acid sequence data. Analytical Biochemistry, 182, 319-326.
    • (1989) Analytical Biochemistry , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 16
    • 75649095700 scopus 로고    scopus 로고
    • Phytolacca americana lectin (Pa-2; pokeweed mitogen): an intrinsically unordered protein and its conversion to partial order at low pH
    • Ahmad, E., Rahman, S. K., Khan, J. M., Varshney, A., & Khan, R. H. (2010). Phytolacca americana lectin (Pa-2; pokeweed mitogen): an intrinsically unordered protein and its conversion to partial order at low pH. Bioscience Reports, 30, 125-134.
    • (2010) Bioscience Reports , vol.30 , pp. 125-134
    • Ahmad, E.1    Rahman, S.K.2    Khan, J.M.3    Varshney, A.4    Khan, R.H.5
  • 17
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the web: A case study using the Phyre server
    • Kelley, L. A., & Sternberg, M. J. E. (2009). Protein structure prediction on the web: A case study using the Phyre server. Nature Protocols, 4, 363-371.
    • (2009) Nature Protocols , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 18
    • 0034624021 scopus 로고    scopus 로고
    • Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures
    • Bhattacharya, A. A., Curry, S., & Franks, N. P. (2000). Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures. Journal of Biological Chemistry, 275, 38731-38738.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 38731-38738
    • Bhattacharya, A.A.1    Curry, S.2    Franks, N.P.3
  • 19
    • 48449099381 scopus 로고    scopus 로고
    • PBEQ-Solver for online visualization of electrostatic potential of biomolecules
    • Jo, S., Vargyas, M., Vasko-Szedlar, J., Roux, B., & Im, W. (2008). PBEQ-Solver for online visualization of electrostatic potential of biomolecules. Nucleic Acids Research, 36, W270-W275.
    • (2008) Nucleic Acids Research , vol.36
    • Jo, S.1    Vargyas, M.2    Vasko-Szedlar, J.3    Roux, B.4    Im, W.5
  • 22
    • 0030203863 scopus 로고    scopus 로고
    • TREEVIEW: An application to display phylogenetic trees on personal computers
    • Page, R. D. M. (1996). TREEVIEW: An application to display phylogenetic trees on personal computers. Computer Applications in the Biosciences, 12, 357-358.
    • (1996) Computer Applications in the Biosciences , vol.12 , pp. 357-358
    • Page, R.D.M.1
  • 23
    • 33644847172 scopus 로고    scopus 로고
    • Prediction of protein stability changes for single-site mutations using support vector machines
    • Cheng, J., Randall, A., & Baldi, P. (2005). Prediction of protein stability changes for single-site mutations using support vector machines. Proteins, 62, 1125-1132.
    • (2005) Proteins , vol.62 , pp. 1125-1132
    • Cheng, J.1    Randall, A.2    Baldi, P.3
  • 24
    • 33747838537 scopus 로고    scopus 로고
    • CUPSAT: Prediction of protein stability upon point mutations
    • Parthiban, V., Gromiha, M. M., & Schomburg, D. (2006). CUPSAT: Prediction of protein stability upon point mutations. Nucleic Acids Research, 34, W239-W242.
    • (2006) Nucleic Acids Research , vol.34
    • Parthiban, V.1    Gromiha, M.M.2    Schomburg, D.3
  • 25
    • 0031808804 scopus 로고    scopus 로고
    • Chemical denaturation: potential impact of undetected intermediates in the free energy of unfolding and m-values obtained from a two-state assumption
    • Soulages, J. L. (1998). Chemical denaturation: potential impact of undetected intermediates in the free energy of unfolding and m-values obtained from a two-state assumption. Biophysical Journal, 75, 484-492.
    • (1998) Biophysical Journal , vol.75 , pp. 484-492
    • Soulages, J.L.1
  • 27
  • 28
    • 0034687724 scopus 로고    scopus 로고
    • Equilibrium and kinetic studies on folding of the authentic and recombinant forms of human alpha-lactalbumin by circular dichroism spectroscopy
    • Chaudhuri, T. K., Arai, M., Terada, T. P., Ikura, T., & Kuwajima, K. (2000). Equilibrium and kinetic studies on folding of the authentic and recombinant forms of human alpha-lactalbumin by circular dichroism spectroscopy. Biochemistry, 39, 15643-15651.
    • (2000) Biochemistry , vol.39 , pp. 15643-15651
    • Chaudhuri, T.K.1    Arai, M.2    Terada, T.P.3    Ikura, T.4    Kuwajima, K.5
  • 29
    • 0032096837 scopus 로고    scopus 로고
    • Continuum solvation model: computation of electrostatic forces from numerical solutions to the Poisson-Boltzmann equation
    • Im, W., Beglov, D., & Roux, B. (1998). Continuum solvation model: computation of electrostatic forces from numerical solutions to the Poisson-Boltzmann equation. Computer Physics Communications, 111, 59-75.
    • (1998) Computer Physics Communications , vol.111 , pp. 59-75
    • Im, W.1    Beglov, D.2    Roux, B.3
  • 30
    • 0017166109 scopus 로고
    • Reversible unfolding of the major fraction of ovalbumin by guanidine hydrochloride
    • Ahmad, F., & Salahuddin, A. (1976). Reversible unfolding of the major fraction of ovalbumin by guanidine hydrochloride. Biochemistry, 15, 5168-5175.
    • (1976) Biochemistry , vol.15 , pp. 5168-5175
    • Ahmad, F.1    Salahuddin, A.2
  • 31
    • 0032751222 scopus 로고    scopus 로고
    • Thermodynamic features of the chemical and thermal denaturations of human serum albumin
    • Farruggia, B., & Pico, G. A. (1999). Thermodynamic features of the chemical and thermal denaturations of human serum albumin. International Journal of Biological Macromolecules, 26, 317-323.
    • (1999) International Journal of Biological Macromolecules , vol.26 , pp. 317-323
    • Farruggia, B.1    Pico, G.A.2
  • 35
    • 0035510132 scopus 로고    scopus 로고
    • Defective nephrin trafficking caused by missense mutations in the NPHS1 gene: Insight into the mechanisms of congenital nephrotic syndrome
    • Liu, L., Doné, S. C., Khoshnoodi, J., Bertorello, A., Wartiovaara, J., Berggren, P. O., et al. (2001). Defective nephrin trafficking caused by missense mutations in the NPHS1 gene: Insight into the mechanisms of congenital nephrotic syndrome. Human Molecular Genetics, 10, 2637-2644.
    • (2001) Human Molecular Genetics , vol.10 , pp. 2637-2644
    • Liu, L.1    Doné, S.C.2    Khoshnoodi, J.3    Bertorello, A.4    Wartiovaara, J.5    Berggren, P.O.6    Tryggvason, K.7
  • 37
    • 34248640314 scopus 로고    scopus 로고
    • Effect of physiological concentration of urea on the conformation of human serum albumin
    • Gull, N., Sen, P., & Kabir-Ud-Din, Khan. R. H. (2007). Effect of physiological concentration of urea on the conformation of human serum albumin. Journal of Biochemistry, 141, 261-268.
    • (2007) Journal of Biochemistry , vol.141 , pp. 261-268
    • Gull, N.1    Sen, P.2    Kabir-Ud-Din3    Khan, R.H.4
  • 38
    • 84965086162 scopus 로고
    • Titration of bovine serum albumin in urea and in formaldehyde solutions
    • Levy, M. (1958). Titration of bovine serum albumin in urea and in formaldehyde solutions. Comptes Rendus des Travaux du Laboratoire Carlsberg, 30, 301-308.
    • (1958) Comptes Rendus Des Travaux Du Laboratoire Carlsberg , vol.30 , pp. 301-308
    • Levy, M.1
  • 39
    • 70349132068 scopus 로고    scopus 로고
    • Urea-induced denaturation process on defatted human serum albumin and in the presence of palmitic acid
    • Leggio, C., Galantini, L., Konarev, P. V., & Pavel, N. V. (2009). Urea-induced denaturation process on defatted human serum albumin and in the presence of palmitic acid. Journal of Physical Chemistry B, 113, 12590-12602.
    • (2009) Journal of Physical Chemistry B , vol.113 , pp. 12590-12602
    • Leggio, C.1    Galantini, L.2    Konarev, P.V.3    Pavel, N.V.4
  • 40
    • 0026788012 scopus 로고
    • Water as ligand: preferential binding and exclusion of denaturants in protein unfolding
    • Timasheff, S. (1992). Water as ligand: preferential binding and exclusion of denaturants in protein unfolding. Biochemistry, 31, 9857-9864.
    • (1992) Biochemistry , vol.31 , pp. 9857-9864
    • Timasheff, S.1
  • 41
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers, J. K., Pace, C. N., & Scholtz, J. (1995). Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding. Protein Science, 4, 2138-2148.
    • (1995) Protein Science , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.3
  • 42
    • 67650363919 scopus 로고    scopus 로고
    • Urea impedes the hydrophobic collapse of partially unfolded proteins
    • Stumpe, M. C., & Grubmuller, H. (2009). Urea impedes the hydrophobic collapse of partially unfolded proteins. Biophysical Journal, 96, 3744-3752.
    • (2009) Biophysical Journal , vol.96 , pp. 3744-3752
    • Stumpe, M.C.1    Grubmuller, H.2
  • 43
    • 0037133522 scopus 로고    scopus 로고
    • Divalent cation induced changes in structural properties of the dimeric enzyme glucose oxidase: Dual effect of dimer stabilization and dissociation with loss of cooperative interactions in enzyme monomer
    • Akhtar, M. S., Ahmad, A., & Bhakuni, V. (2002). Divalent cation induced changes in structural properties of the dimeric enzyme glucose oxidase: Dual effect of dimer stabilization and dissociation with loss of cooperative interactions in enzyme monomer. Biochemistry, 41, 3819-3827.
    • (2002) Biochemistry , vol.41 , pp. 3819-3827
    • Akhtar, M.S.1    Ahmad, A.2    Bhakuni, V.3
  • 44
    • 0001664170 scopus 로고
    • The effect of compounds of the urea-guanidinium class on the activity coefficient of acetyltetraglycine ethyl ester and related compounds
    • Robinson, D. R., & Jencks, W. P. (1965). The effect of compounds of the urea-guanidinium class on the activity coefficient of acetyltetraglycine ethyl ester and related compounds. Journal of the American Chemical Society, 87, 2462-2470.
    • (1965) Journal of the American Chemical Society , vol.87 , pp. 2462-2470
    • Robinson, D.R.1    Jencks, W.P.2
  • 45
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C. N. (1986). Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods in Enzymology, 131, 266-280.
    • (1986) Methods in Enzymology , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 46
    • 0027730340 scopus 로고
    • Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A
    • Mayo, S. L., & Baldwin, R. L. (1993). Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A. Science, 262, 873-876.
    • (1993) Science , vol.262 , pp. 873-876
    • Mayo, S.L.1    Baldwin, R.L.2
  • 47
    • 0028569153 scopus 로고
    • Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions
    • Monera, O. D., Kay, C. M., & Hodges, R. S. (1994). Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions. Protein Science, 3, 1984-1991.
    • (1994) Protein Science , vol.3 , pp. 1984-1991
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 48
    • 34250869055 scopus 로고    scopus 로고
    • Interactions between hydrophobic and ionic solutes in aqueous guanidinium chloride and urea solutions: Lessons for protein denaturation mechanism
    • O'Brien, E. P., Dima, R. I., Brooks, B., & Thirumalai, D. (2007). Interactions between hydrophobic and ionic solutes in aqueous guanidinium chloride and urea solutions: Lessons for protein denaturation mechanism. Journal of the American Chemical Society, 129, 7346-7353.
    • (2007) Journal of the American Chemical Society , vol.129 , pp. 7346-7353
    • O'Brien, E.P.1    Dima, R.I.2    Brooks, B.3    Thirumalai, D.4
  • 49
    • 0141748498 scopus 로고    scopus 로고
    • Energetic and structural analysis of the role of tryptophan 59 in FKBP12
    • Fulton, K. F., Jackson, S. E., & Buckle, A. M. (2003). Energetic and structural analysis of the role of tryptophan 59 in FKBP12. Biochemistry, 42, 2364-2372.
    • (2003) Biochemistry , vol.42 , pp. 2364-2372
    • Fulton, K.F.1    Jackson, S.E.2    Buckle, A.M.3
  • 51
    • 0025337398 scopus 로고
    • Role of arginine 67 in the stabilization of chymotrypsin inhibitor 2: Examination of amide proton exchange rates and denaturation thermodynamics of an engineered protein
    • Jandu, S. K., Ray, S., Brooks, L., & Leatherbarrow, R. J. (1990). Role of arginine 67 in the stabilization of chymotrypsin inhibitor 2: Examination of amide proton exchange rates and denaturation thermodynamics of an engineered protein. Biochemistry, 29, 6264-6269.
    • (1990) Biochemistry , vol.29 , pp. 6264-6269
    • Jandu, S.K.1    Ray, S.2    Brooks, L.3    Leatherbarrow, R.J.4
  • 52
    • 0032813558 scopus 로고    scopus 로고
    • A lysine-to-arginine change found in natural alleles of the human T-cell lymphotropic/leukemia virus type 1 p12(I) protein greatly influences its stability
    • Trovato, R., Mulloy, J. C., Johnson, J. M., Takemoto, S., de Oliveira, M. P., & Franchini, G. (1999). A lysine-to-arginine change found in natural alleles of the human T-cell lymphotropic/leukemia virus type 1 p12(I) protein greatly influences its stability. Journal of Virology, 73, 6460-6467.
    • (1999) Journal of Virology , vol.73 , pp. 6460-6467
    • Trovato, R.1    Mulloy, J.C.2    Johnson, J.M.3    Takemoto, S.4    de Oliveira, M.P.5    Franchini, G.6
  • 53
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • Vogt, G., Woell, S., & Argos, P. (1997). Protein thermal stability, hydrogen bonds, and ion pairs. Journal of Molecular Biology, 269, 631-643.
    • (1997) Journal of Molecular Biology , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3


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