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Volumn 99, Issue 4, 2010, Pages 1157-1165

Thermal and structural stability of adsorbed proteins

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EID: 77958171872     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.05.030     Document Type: Article
Times cited : (30)

References (40)
  • 1
    • 33751155475 scopus 로고
    • Computer simulation of hydro-phobic hydration forces on stacked plates at short range
    • Wallqvist, A., and B. J. Berne. 1995. Computer simulation of hydro-phobic hydration forces on stacked plates at short range. J. Phys. Chem. 99:2893-2899.
    • (1995) J. Phys. Chem. , vol.99 , pp. 2893-2899
    • Wallqvist, A.1    Berne, B.J.2
  • 2
    • 0011960339 scopus 로고    scopus 로고
    • Hydrophobicity at small and large length scales
    • Lum, K., D. Chandler, and J. D. Weeks. 1999. Hydrophobicity at small and large length scales. J. Phys. Chem. B. 103:4570-4577.
    • (1999) J. Phys. Chem. B. , vol.103 , pp. 4570-4577
    • Lum, K.1    Chandler, D.2    Weeks, J.D.3
  • 3
    • 65249175791 scopus 로고    scopus 로고
    • How interfaces affect hydrophobically driven polymer folding
    • Jamadagni, S. N., R. Godawat, ..., S. Garde. 2009. How interfaces affect hydrophobically driven polymer folding. J. Phys. Chem. B. 113:4093-4101.
    • (2009) J. Phys. Chem. B. , vol.113 , pp. 4093-4101
    • Jamadagni, S.N.1    Godawat, R.2    Garde, S.3
  • 4
    • 0035799395 scopus 로고    scopus 로고
    • Adsorption of IgG onto hydrophobic Teflon. Differences between the F(ab) and F (c) domains
    • Vermeer, A. W. P., C. E. Giacomelli, and W. Norde. 2001. Adsorption of IgG onto hydrophobic Teflon. Differences between the F(ab) and F (c) domains. Biochim. Biophys. Acta. 1526:61-69.
    • (2001) Biochim. Biophys. Acta. , vol.1526 , pp. 61-69
    • Vermeer, A.W.P.1    Giacomelli, C.E.2    Norde, W.3
  • 5
    • 0033275324 scopus 로고    scopus 로고
    • Conformational changes in proteins at interfaces: From solution to the interface, and back
    • Norde, W., and C. E. Giacomelli. 1999. Conformational changes in proteins at interfaces: from solution to the interface, and back. Macro-mol. Symp. 145:125-136.
    • (1999) Macro-mol. Symp. , vol.145 , pp. 125-136
    • Norde, W.1    Giacomelli, C.E.2
  • 6
  • 7
    • 29244452592 scopus 로고    scopus 로고
    • Interfacial adsorption of insulin conformational changes and reversibility of adsorption
    • Mollmann, S. H., L. Jorgensen, ..., S. Frokjaer. 2006. Interfacial adsorption of insulin conformational changes and reversibility of adsorption. Eur. J. Pharm. Sci. 27:194-204.
    • (2006) Eur. J. Pharm. Sci. , vol.27 , pp. 194-204
    • Mollmann, S.H.1    Jorgensen, L.2    Frokjaer, S.3
  • 8
    • 0345688752 scopus 로고    scopus 로고
    • Influence of hydrophobic Teflon particles on the structure of amyloid b-peptide
    • Giacomelli, C. E., and W. Norde. 2003. Influence of hydrophobic Teflon particles on the structure of amyloid b-peptide. Biomacromole-cules. 4:1719-1726.
    • (2003) Biomacromole-cules , vol.4 , pp. 1719-1726
    • Giacomelli, C.E.1    Norde, W.2
  • 9
    • 20444488480 scopus 로고    scopus 로고
    • Conformational changes of the amyloid b-peptide (1-40) adsorbed on solid surfaces
    • Giacomelli, C. E., and W. Norde. 2005. Conformational changes of the amyloid b-peptide (1-40) adsorbed on solid surfaces. Macromol. Bio-sci. 5:401-407.
    • (2005) Macromol. Bio-sci. , vol.5 , pp. 401-407
    • Giacomelli, C.E.1    Norde, W.2
  • 10
    • 0036231053 scopus 로고    scopus 로고
    • Structural changes and molecular interactions of hydrophobin SC3 in solution and on a hydrophobic surface
    • Wang, X., M. L. de Vocht, ..., G. T. Robillard. 2002. Structural changes and molecular interactions of hydrophobin SC3 in solution and on a hydrophobic surface. Protein Sci. 11:1172-1181.
    • (2002) Protein Sci , vol.11 , pp. 1172-1181
    • Wang, X.1    De Vocht, M.L.2    Robillard, G.T.3
  • 11
    • 0031919678 scopus 로고    scopus 로고
    • Structural characterization of the hydrophobin SC3, as a monomer and after self-assembly at hydrophobic/hydrophilic interfaces
    • de Vocht, M. L., K. Scholtmeijer, ..., G. T. Robillard. 1998. Structural characterization of the hydrophobin SC3, as a monomer and after self-assembly at hydrophobic/hydrophilic interfaces. Biophys. J. 74: 2059-2068.
    • (1998) Biophys. J. , vol.74 , pp. 2059-2068
    • De Vocht, M.L.1    Scholtmeijer, K.2    Robillard, G.T.3
  • 12
    • 0031574008 scopus 로고    scopus 로고
    • Adsorption-induced conformational changes in the serine proteinase savinase: A tryptophan fluorescence and circular dichroism study
    • Maste, M. C. L., W. Norde, and A. J. W. G. Visser. 1997. Adsorption-induced conformational changes in the serine proteinase savinase: a tryptophan fluorescence and circular dichroism study. J. Colloid Interface Sci. 196:224-230.
    • (1997) J. Colloid Interface Sci , vol.196 , pp. 224-230
    • Maste, M.C.L.1    Norde, W.2    Visser, A.J.W.G.3
  • 13
    • 0035888421 scopus 로고    scopus 로고
    • FT-IR analysis of BSA fouled on ultrafiltration and microfiltration membranes
    • Maruyama, T., S. Katoh, ..., K. Satoh. 2001. FT-IR analysis of BSA fouled on ultrafiltration and microfiltration membranes. J. Membr. Sci. 192:201-207.
    • (2001) J. Membr. Sci. , vol.192 , pp. 201-207
    • Maruyama, T.1    Katoh, S.2    Satoh, K.3
  • 14
    • 21244462685 scopus 로고    scopus 로고
    • Protein structural perturbation and aggregation on homogeneous surfaces
    • Sethuraman, A., and G. Belfort. 2005. Protein structural perturbation and aggregation on homogeneous surfaces. Biophys. J. 88:1322-1333.
    • (2005) Biophys. J. , vol.88 , pp. 1322-1333
    • Sethuraman, A.1    Belfort, G.2
  • 15
    • 4043104043 scopus 로고    scopus 로고
    • Protein unfolding at interfaces: Slow dynamics of a-helix to b-sheet transition
    • Sethuraman, A., G. Vedantham, ..., G. Belfort. 2004. Protein unfolding at interfaces: slow dynamics of a-helix to b-sheet transition. Proteins: Struct. Funct. Bioinf. 56:669-678.
    • (2004) Proteins: Struct. Funct. Bioinf. , vol.56 , pp. 669-678
    • Sethuraman, A.1    Vedantham, G.2    Belfort, G.3
  • 16
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K. A. 1990. Dominant forces in protein folding. Biochemistry. 29:7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 17
    • 0029251458 scopus 로고
    • Structures and stabilities of adsorbed proteins
    • Haynes, C. A., and W. Norde. 1995. Structures and stabilities of adsorbed proteins. J. Colloid Interface Sci. 169:313-328.
    • (1995) J. Colloid Interface Sci , vol.169 , pp. 313-328
    • Haynes, C.A.1    Norde, W.2
  • 18
    • 0034436051 scopus 로고    scopus 로고
    • Buried charged surface in proteins
    • Kajander, T., P. C. Kahn, ..., A. Goldman. 2000. Buried charged surface in proteins. Structure. 8:1203-1214.
    • (2000) Structure , vol.8 , pp. 1203-1214
    • Kajander, T.1    Kahn, P.C.2    Goldman, A.3
  • 19
    • 0028929583 scopus 로고
    • Free energy balance in protein folding
    • Honig, B., and A. S. Yang. 1995. Free energy balance in protein folding. Adv. Protein Chem. 46:27-58.
    • (1995) Adv. Protein Chem , vol.46 , pp. 27-58
    • Honig, B.1    Yang, A.S.2
  • 20
    • 0028950075 scopus 로고
    • Forces of tertiary structural organization in globular proteins
    • Yue, K., and K. A. Dill. 1995. Forces of tertiary structural organization in globular proteins. Proc. Natl. Acad. Sci. USA. 92:146-150.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 146-150
    • Yue, K.1    Dill, K.A.2
  • 21
    • 53449101250 scopus 로고    scopus 로고
    • Finite size effects on locating conformational transitions for macromolecules
    • Sharma, S., and S. K. Kumar. 2008. Finite size effects on locating conformational transitions for macromolecules. J. Chem. Phys. 129:134901.
    • (2008) J. Chem. Phys. , vol.129 , pp. 134901
    • Sharma, S.1    Kumar, S.K.2
  • 22
    • 0028224689 scopus 로고
    • Modeling compact denatured states of proteins
    • Lattman, E. E., K. M. Fiebig, and K. A. Dill. 1994. Modeling compact denatured states of proteins. Biochemistry. 33:6158-6166.
    • (1994) Biochemistry , vol.33 , pp. 6158-6166
    • Lattman, E.E.1    Fiebig, K.M.2    Dill, K.A.3
  • 23
    • 23844465903 scopus 로고    scopus 로고
    • Protein-folding landscapes in multichain systems
    • Cellmer, T., D. Bratko, ..., H. Blanch. 2005. Protein-folding landscapes in multichain systems. Proc. Natl. Acad. Sci. USA. 102:11692-11697.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 11692-11697
    • Cellmer, T.1    Bratko, D.2    Blanch, H.3
  • 24
    • 41349094526 scopus 로고    scopus 로고
    • Surface-induced conformational changes in lattice model proteins by Monte Carlo simulation
    • Castells, V., S. X. Yang, and P. R. Van Tassel. 2002. Surface-induced conformational changes in lattice model proteins by Monte Carlo simulation. Phys. Rev. E Stat. Nonlin. Soft Matter Phys. 65:031912.
    • (2002) Phys. Rev. e Stat. Nonlin. Soft Matter Phys. , vol.65 , pp. 031912
    • Castells, V.1    Yang, S.X.2    Van Tassel, P.R.3
  • 25
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules. 1. the method
    • Kumar, S., D. Bouzida, ..., J. M. Rosenberg. 1992. The weighted histogram analysis method for free-energy calculations on biomolecules. 1. The method. J. Comput. Chem. 13:1011-1021.
    • (1992) J. Comput. Chem. , vol.13 , pp. 1011-1021
    • Kumar, S.1    Bouzida, D.2    Rosenberg, J.M.3
  • 26
    • 33646987405 scopus 로고
    • Optimized Monte Carlo data analysis
    • Ferrenberg, A. M., and R. H. Swendsen. 1989. Optimized Monte Carlo data analysis. Phys. Rev. Lett. 63:1195-1198.
    • (1989) Phys. Rev. Lett. , vol.63 , pp. 1195-1198
    • Ferrenberg, A.M.1    Swendsen, R.H.2
  • 27
    • 33947398571 scopus 로고    scopus 로고
    • Use of the weighted histogram analysis method for the analysis of simulated and parallel tempering simulations
    • Chodera, J. D., W. C. Swope, ..., K. A. Dill. 2007. Use of the weighted histogram analysis method for the analysis of simulated and parallel tempering simulations. J. Chem. Theory Comput. 3:26-41.
    • (2007) J. Chem. Theory Comput , vol.3 , pp. 26-41
    • Chodera, J.D.1    Swope, W.C.2    Dill, K.A.3
  • 29
    • 0000179346 scopus 로고
    • Analysis of Monte-Carlo results on kinetics of lattice polymer-chains with excluded volume
    • Hilhorst, H. J., and J. M. Deutch. 1975. Analysis of Monte-Carlo results on kinetics of lattice polymer-chains with excluded volume. J. Chem. Phys. 63:5153-5161.
    • (1975) J. Chem. Phys. , vol.63 , pp. 5153-5161
    • Hilhorst, H.J.1    Deutch, J.M.2
  • 30
    • 78650612270 scopus 로고
    • Configurational bias Monte-Carlo-a new sampling scheme for flexible chains
    • Siepmann, J. I., and D. Frenkel. 1992. Configurational bias Monte-Carlo-a new sampling scheme for flexible chains. Mol. Phys. 75:59-70.
    • (1992) Mol. Phys. , vol.75 , pp. 59-70
    • Siepmann, J.I.1    Frenkel, D.2
  • 31
    • 0001699086 scopus 로고    scopus 로고
    • Transition path sampling: Throwing ropes over mountains in the dark
    • Bolhuis, P. G., C. Dellago, ..., D. Chandler. 2000. Transition path sampling: throwing ropes over mountains in the dark. J. Phys. Condens. Matter. 12:A147-A152.
    • (2000) J. Phys. Condens. Matter. , vol.12
    • Bolhuis, P.G.1    Dellago, C.2    Chandler, D.3
  • 32
    • 0005610602 scopus 로고
    • Empirical-studies of hydro-phobicity 2. Distribution of the hydrophobic, hydrophilic, neutral, and ambivalent amino-acids in the interior and exterior layers of native proteins
    • Meirovitch, H., and H. A. Scheraga. 1980. Empirical-studies of hydro-phobicity. 2. Distribution of the hydrophobic, hydrophilic, neutral, and ambivalent amino-acids in the interior and exterior layers of native proteins. Macromolecules. 13:1406-1414.
    • (1980) Macromolecules , vol.13 , pp. 1406-1414
    • Meirovitch, H.1    Scheraga, H.A.2
  • 33
    • 0000433840 scopus 로고
    • Surface-induced enhancement of internal structure in polymers and proteins
    • Wattenbarger, M. R., H. S. Chan, ..., K. A. Dill. 1990. Surface-induced enhancement of internal structure in polymers and proteins. J. Chem. Phys. 93:8343-8351.
    • (1990) J. Chem. Phys. , vol.93 , pp. 8343-8351
    • Wattenbarger, M.R.1    Chan, H.S.2    Dill, K.A.3
  • 34
    • 0000667437 scopus 로고
    • Enhanced structure in polymers at interfaces
    • Chan, H. S., M. R. Wattenbarger, ..., K. A. Dill. 1991. Enhanced structure in polymers at interfaces. J. Chem. Phys. 94:8542-8557.
    • (1991) J. Chem. Phys. , vol.94 , pp. 8542-8557
    • Chan, H.S.1    Wattenbarger, M.R.2    Dill, K.A.3
  • 35
    • 0033150721 scopus 로고    scopus 로고
    • Computer simulation of competition between protein folding and aggregation
    • Gupta, P., C. K. Hall, and A. Voegler. 1999. Computer simulation of competition between protein folding and aggregation. Fluid Phase Equilib. 158:87-93.
    • (1999) Fluid Phase Equilib , vol.158 , pp. 87-93
    • Gupta, P.1    Hall, C.K.2    Voegler, A.3
  • 36
    • 0035949430 scopus 로고    scopus 로고
    • Stabilization of proteins in confined spaces
    • Zhou, H. X., and K. A. Dill. 2001. Stabilization of proteins in confined spaces. Biochemistry. 40:11289-11293.
    • (2001) Biochemistry , vol.40 , pp. 11289-11293
    • Zhou, H.X.1    Dill, K.A.2
  • 37
    • 3543054174 scopus 로고    scopus 로고
    • Forced folding and structural analysis of metastable proteins
    • Peterson, R. W., K. Anbalagan, ..., A. J. Wand. 2004. Forced folding and structural analysis of metastable proteins. J. Am. Chem. Soc. 126:9498-9499.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 9498-9499
    • Peterson, R.W.1    Anbalagan, K.2    Wand, A.J.3
  • 38
    • 4644332696 scopus 로고    scopus 로고
    • Protein encapsulation in mesoporous silicate: The effects of confinement on protein stability, hydration, and volumetric properties
    • Ravindra, R., S. Zhao, ..., R. Winter. 2004. Protein encapsulation in mesoporous silicate: the effects of confinement on protein stability, hydration, and volumetric properties. J. Am. Chem. Soc. 126: 12224-12225.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 12224-12225
    • Ravindra, R.1    Zhao, S.2    Winter, R.3
  • 39
    • 34447519151 scopus 로고    scopus 로고
    • Enhanced stability of enzymes adsorbed onto nanoparticles
    • Asuri, P., S. S. Karajanagi, ..., R. S. Kane. 2007. Enhanced stability of enzymes adsorbed onto nanoparticles. J. Nanosci. Nanotechnol. 7:1675-1678.
    • (2007) J. Nanosci. Nanotechnol. , vol.7 , pp. 1675-1678
    • Asuri, P.1    Karajanagi, S.S.2    Kane, R.S.3
  • 40
    • 70349090176 scopus 로고    scopus 로고
    • Enhancing protein stability by adsorption onto raftlike lipid domains
    • Litt, J., C. Padala, ..., R. S. Kane. 2009. Enhancing protein stability by adsorption onto raftlike lipid domains. J. Am. Chem. Soc. 131: 7107-7111.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 7107-7111
    • Litt, J.1    Padala, C.2    Kane, R.S.3


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