메뉴 건너뛰기




Volumn , Issue , 2013, Pages 49-72

Small-Angle X-Ray Scattering Applied to Proteins in Solution

Author keywords

Bovine serum albumin (BSA); Dilute solution; Guinier's law; Kratky's representation; Old yellow enzyme (OYE); Porod's invariant; Protein aggregation; Protein interaction; Replication factor C (RFC); Small angle X ray scattering (SAXS)

Indexed keywords


EID: 84886338900     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9781118523063.ch3     Document Type: Chapter
Times cited : (16)

References (82)
  • 1
    • 77956190770 scopus 로고    scopus 로고
    • Structural characterization of proteins and complexes using small-angle X-ray solution scattering
    • Mertens HDT, Svergun DI. Structural characterization of proteins and complexes using small-angle X-ray solution scattering. J Struct Biol 2010;172:128-141.
    • (2010) J Struct Biol , vol.172 , pp. 128-141
    • Mertens, H.D.T.1    Svergun, D.I.2
  • 2
    • 0030736871 scopus 로고    scopus 로고
    • Insights into biomolecular function from smallangle scattering
    • Trewhella J. Insights into biomolecular function from smallangle scattering. Curr Opin Struct Biol 1997;7:702-708.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 702-708
    • Trewhella, J.1
  • 3
    • 74049110959 scopus 로고    scopus 로고
    • The importance of protein-protein interactions on the pH-induced conformational changes of bovine serum albumin: a small-angle X-ray scattering study
    • Barbosa LRS, Ortore MG, Spinozzi F, Mariani P, Bernstorff S, Itri R. The importance of protein-protein interactions on the pH-induced conformational changes of bovine serum albumin: a small-angle X-ray scattering study. Biophys J 2010;98(1):147-157.
    • (2010) Biophys J , vol.98 , Issue.1 , pp. 147-157
    • Barbosa, L.R.S.1    Ortore, M.G.2    Spinozzi, F.3    Mariani, P.4    Bernstorff, S.5    Itri, R.6
  • 7
    • 0038024150 scopus 로고    scopus 로고
    • A systematic study of bovine serum albumin (BSA) and sodium dodecyl sulfate (SDS) interactions by electrical conductivity, surface tension and small angle x-ray scattering
    • Santos SF, Zanette D, Fischer H, Itri R. A systematic study of bovine serum albumin (BSA) and sodium dodecyl sulfate (SDS) interactions by electrical conductivity, surface tension and small angle x-ray scattering. J Coll Interf Sci 2003;262:400-408.
    • (2003) J Coll Interf Sci , vol.262 , pp. 400-408
    • Santos, S.F.1    Zanette, D.2    Fischer, H.3    Itri, R.4
  • 9
    • 79952756956 scopus 로고    scopus 로고
    • Structural analysis of protein complexes with sodium alkyl sulfates by small-angle scattering and polyacrylamide gel electrophoresis
    • Ospinal-Jiménez M, Pozzo DC. Structural analysis of protein complexes with sodium alkyl sulfates by small-angle scattering and polyacrylamide gel electrophoresis. Langmuir 2011;27(3):928-935.
    • (2011) Langmuir , vol.27 , Issue.3 , pp. 928-935
    • Ospinal-Jiménez, M.1    Pozzo, D.C.2
  • 10
    • 79958057466 scopus 로고    scopus 로고
    • Structural insights into early folding events using continuous-flow time-resolved small-angle X-ray scattering
    • Kathuria SV, Guo L, Graceffa R, Barrea R, Nobrega P, Matthews R, Irving TC, Bilsel O. Structural insights into early folding events using continuous-flow time-resolved small-angle X-ray scattering. Biopolymers 2011;95(8):550-558.
    • (2011) Biopolymers , vol.95 , Issue.8 , pp. 550-558
    • Kathuria, S.V.1    Guo, L.2    Graceffa, R.3    Barrea, R.4    Nobrega, P.5    Matthews, R.6    Irving, T.C.7    Bilsel, O.8
  • 11
    • 70349411555 scopus 로고    scopus 로고
    • High brilliance small-angle X-ray scattering applied to soft matter
    • Narayanan T. High brilliance small-angle X-ray scattering applied to soft matter. Curr Opin Coll Interf Sci 2009;14(6):409-415.
    • (2009) Curr Opin Coll Interf Sci , vol.14 , Issue.6 , pp. 409-415
    • Narayanan, T.1
  • 12
    • 0032995379 scopus 로고    scopus 로고
    • Reversibility and hierarchy of thermal transition of hen egg-white lysozyme studied by small-angle X-ray scattering
    • Arai S, Hirai M. Reversibility and hierarchy of thermal transition of hen egg-white lysozyme studied by small-angle X-ray scattering. Biophys J 1999;76:2192-2197.
    • (1999) Biophys J , vol.76 , pp. 2192-2197
    • Arai, S.1    Hirai, M.2
  • 13
    • 0003519476 scopus 로고
    • Small-Angle Scattering of X-Rays
    • New York: Wiley & Sons;
    • Guinier A, Fournet G. Small-Angle Scattering of X-Rays. New York: Wiley & Sons; 1955.
    • (1955)
    • Guinier, A.1    Fournet, G.2
  • 14
    • 0001507241 scopus 로고
    • Light scattering of a concentrated multicomponent system of hard spheres in the Percus-Yevick approximation
    • Vrij A. Light scattering of a concentrated multicomponent system of hard spheres in the Percus-Yevick approximation. J Chem Phys 1978;69:1742-47.
    • (1978) J Chem Phys , vol.69 , pp. 1742-1747
    • Vrij, A.1
  • 15
    • 36049052760 scopus 로고
    • Structure of binary liquid mixtures
    • Ashcroft NW, Langreth DC. Structure of binary liquid mixtures. Phys Rev 1967;156:685.
    • (1967) Phys Rev , vol.156 , pp. 685
    • Ashcroft, N.W.1    Langreth, D.C.2
  • 16
    • 0003644127 scopus 로고
    • The Theory of Simple Liquids
    • London: Academic Press
    • Hansen JP, McDonald IR. The Theory of Simple Liquids. London: Academic Press; 1986.
    • (1986)
    • Hansen, J.P.1    McDonald, I.R.2
  • 17
    • 0003702492 scopus 로고
    • Small-Angle X-Ray Scattering
    • London: Academic Press
    • Glatter O, Kratky O. Small-Angle X-Ray Scattering. London: Academic Press; 1982.
    • (1982)
    • Glatter, O.1    Kratky, O.2
  • 18
    • 0027400842 scopus 로고
    • Molten globule of cytochrome c studied by the small angle X-ray scattering
    • Kataoka M, Hagihara Y, Mihara K, Goto Y. Molten globule of cytochrome c studied by the small angle X-ray scattering. J Mol Biol 1993;229:591-596.
    • (1993) J Mol Biol , vol.229 , pp. 591-596
    • Kataoka, M.1    Hagihara, Y.2    Mihara, K.3    Goto, Y.4
  • 19
    • 0029032691 scopus 로고
    • Structural characterization of molten globule and native states of apomyoglobin by solution X-ray scattering
    • Kataoka M, Nishii I, Fujisawa T, Ueki T, Tokunaga F, Goto Y. Structural characterization of molten globule and native states of apomyoglobin by solution X-ray scattering. J Mol Biol 1995;249:215-228.
    • (1995) J Mol Biol , vol.249 , pp. 215-228
    • Kataoka, M.1    Nishii, I.2    Fujisawa, T.3    Ueki, T.4    Tokunaga, F.5    Goto, Y.6
  • 20
    • 35949003667 scopus 로고    scopus 로고
    • Methods in Molecular Biophysics: Structure, Dynamics, Function
    • Cambridge: Cambridge University Press
    • Serdyuk IN, Zaccai NR, Zaccai J. Methods in Molecular Biophysics: Structure, Dynamics, Function. Cambridge: Cambridge University Press; 2007.
    • (2007)
    • Serdyuk, I.N.1    Zaccai, N.R.2    Zaccai, J.3
  • 21
    • 34248397195 scopus 로고    scopus 로고
    • Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering
    • Mylonas E, Svergun DI. Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering. J Appl Cryst 2007;40;s245-s249.
    • (2007) J Appl Cryst , vol.40
    • Mylonas, E.1    Svergun, D.I.2
  • 22
    • 0034484513 scopus 로고    scopus 로고
    • SAXS experiments on absolute scale with Kratky systems using water as a secondary standard
    • Orthaber D, Bergmann A, Glatter O. SAXS experiments on absolute scale with Kratky systems using water as a secondary standard. J Appl Cryst 2000;33:218-225.
    • (2000) J Appl Cryst , vol.33 , pp. 218-225
    • Orthaber, D.1    Bergmann, A.2    Glatter, O.3
  • 23
    • 75649147383 scopus 로고    scopus 로고
    • The molecular weight of proteins in solution can be determined from a single SAXS measurement on a relative scale
    • Fischer H, Oliveira Neto M, Napolitano HB, Craievich AF, Polikarpov I. The molecular weight of proteins in solution can be determined from a single SAXS measurement on a relative scale. J Appl Cryst 2010;43:101-109.
    • (2010) J Appl Cryst , vol.43 , pp. 101-109
    • Fischer, H.1    Oliveira Neto, M.2    Napolitano, H.B.3    Craievich, A.F.4    Polikarpov, I.5
  • 24
    • 4043052976 scopus 로고    scopus 로고
    • Small angle x-ray scattering (SAXS) study of the extracellular hemoglobin of Glossoscolex paulistus. Effect of pH, iron oxidation state, and interaction with anionic SDS surfactant
    • Gelamo EL, Itri R, Tabak M. Small angle x-ray scattering (SAXS) study of the extracellular hemoglobin of Glossoscolex paulistus. Effect of pH, iron oxidation state, and interaction with anionic SDS surfactant. J Biol Chem 2004;279:33298-33305.
    • (2004) J Biol Chem , vol.279 , pp. 33298-33305
    • Gelamo, E.L.1    Itri, R.2    Tabak, M.3
  • 25
    • 79952102913 scopus 로고    scopus 로고
    • Conformational studies of peanut agglutinin using small angle X-ray scattering
    • Campana PT, Barbosa LRS, Itri R. Conformational studies of peanut agglutinin using small angle X-ray scattering. Int J Biol Macromol 2011;48(3):398-402.
    • (2011) Int J Biol Macromol , vol.48 , Issue.3 , pp. 398-402
    • Campana, P.T.1    Barbosa, L.R.S.2    Itri, R.3
  • 26
    • 4043111273 scopus 로고    scopus 로고
    • Smallangle X-ray scattering and electron paramagnetic resonance study of the interaction of bovine serum albumin with ionic surfactants
    • Gelamo EL, Itri R, Alonso A, da Silva JV, Tabak M. Smallangle X-ray scattering and electron paramagnetic resonance study of the interaction of bovine serum albumin with ionic surfactants. J Coll Interf Sci 2004;277:471-482.
    • (2004) J Coll Interf Sci , vol.277 , pp. 471-482
    • Gelamo, E.L.1    Itri, R.2    Alonso, A.3    Da Silva, J.V.4    Tabak, M.5
  • 27
    • 77956081477 scopus 로고    scopus 로고
    • Isoelectric point determination for glossoscolex paulistus extracellular hemoglobin: oligomeric stability in acidic pH and relevance to protein-surfactant interactions
    • Santiago PS, Carvalho FAO, Domingues MM, Carvalho JWP, Santos NC, Tabak M. Isoelectric point determination for glossoscolex paulistus extracellular hemoglobin: oligomeric stability in acidic pH and relevance to protein-surfactant interactions. Langmuir 2010;26(12):9794-9801.
    • (2010) Langmuir , vol.26 , Issue.12 , pp. 9794-9801
    • Santiago, P.S.1    Carvalho, F.A.O.2    Domingues, M.M.3    Carvalho, J.W.P.4    Santos, N.C.5    Tabak, M.6
  • 28
    • 2442444146 scopus 로고    scopus 로고
    • Effect of urea on bovine serum albumin in aqueous and reverse micelle environment as investigated by small angle X-ray scattering, fluorescence and circular dicroism
    • Itri R, Caetano W, Barbosa LRS, Baptista MS. Effect of urea on bovine serum albumin in aqueous and reverse micelle environment as investigated by small angle X-ray scattering, fluorescence and circular dicroism. Brasil J Phys 2004;34: 55-63.
    • (2004) Brasil J Phys , vol.34 , pp. 55-63
    • Itri, R.1    Caetano, W.2    Barbosa, L.R.S.3    Baptista, M.S.4
  • 30
    • 58049215425 scopus 로고    scopus 로고
    • Silk fiber assembly studied by synchrotron radiation SAXS/WAXS and Raman spectroscopy
    • Martel A, Burghammer M, Davies RJ, Di Cola E, Vendrely C, Riekel C. Silk fiber assembly studied by synchrotron radiation SAXS/WAXS and Raman spectroscopy. J Am Chem Soc 2008;130:17070-17074.
    • (2008) J Am Chem Soc , vol.130 , pp. 17070-17074
    • Martel, A.1    Burghammer, M.2    Davies, R.J.3    Di Cola, E.4    Vendrely, C.5    Riekel, C.6
  • 32
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun DI. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J Appl Crystallogr 1992;25:495-503.
    • (1992) J Appl Crystallogr , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 33
    • 0034503642 scopus 로고    scopus 로고
    • Solving the indirect Fourier transformation including the structure factor requires a nonlinear least-squares approach. The Boltzmann simplex simulated annealing proves to be very efficient for this task
    • Bergmann A, Fritz G, Glatter O. Solving the indirect Fourier transformation including the structure factor requires a nonlinear least-squares approach. The Boltzmann simplex simulated annealing proves to be very efficient for this task. J Appl Cryst 2000;33:1212-1216.
    • (2000) J Appl Cryst , vol.33 , pp. 1212-1216
    • Bergmann, A.1    Fritz, G.2    Glatter, O.3
  • 34
    • 0029185933 scopus 로고
    • CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun DI, Barberato C, Koch MHJ. CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J Appl Cryst 1995;28:768-773.
    • (1995) J Appl Cryst , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 35
    • 0036213334 scopus 로고    scopus 로고
    • Interaction of proteins in solution from small angle scattering: a perturbative approach
    • Spinozzi F, Gazzillo D, Giacometti A, Mariani P, Carsughi F. Interaction of proteins in solution from small angle scattering: a perturbative approach. Biophys J 2002;82:2165-2175.
    • (2002) Biophys J , vol.82 , pp. 2165-2175
    • Spinozzi, F.1    Gazzillo, D.2    Giacometti, A.3    Mariani, P.4    Carsughi, F.5
  • 37
    • 0000933071 scopus 로고
    • Calculation of small-angle scattering profiles using Monte Carlo simulation
    • Hansen S. Calculation of small-angle scattering profiles using Monte Carlo simulation. J Appl Cryst 1990;23:344-346.
    • (1990) J Appl Cryst , vol.23 , pp. 344-346
    • Hansen, S.1
  • 39
    • 0035193329 scopus 로고    scopus 로고
    • Structural characterization of the pH-denatured states of ferricytochrome-c by synchrotron small angle X-ray scattering
    • Cinelli S, Spinozzi F, Itri R, Finet S, Carsughi F, Onori G, Mariani P. Structural characterization of the pH-denatured states of ferricytochrome-c by synchrotron small angle X-ray scattering. Biophys J 2001;81:3522-3533.
    • (2001) Biophys J , vol.81 , pp. 3522-3533
    • Cinelli, S.1    Spinozzi, F.2    Itri, R.3    Finet, S.4    Carsughi, F.5    Onori, G.6    Mariani, P.7
  • 40
    • 0034046724 scopus 로고    scopus 로고
    • Ligand-induced conformational changes in tissue transglutaminase: Monte Carlo analysis of small-angle scattering data
    • Mariani P, Carsughi F, Spinozzi F, Romanzetti S, Meier G, Casadio R, Bergamini CM. Ligand-induced conformational changes in tissue transglutaminase: Monte Carlo analysis of small-angle scattering data. Biophys J 2000;78:3240.
    • (2000) Biophys J , vol.78 , pp. 3240
    • Mariani, P.1    Carsughi, F.2    Spinozzi, F.3    Romanzetti, S.4    Meier, G.5    Casadio, R.6    Bergamini, C.M.7
  • 41
    • 0034515636 scopus 로고    scopus 로고
    • SAS from inhomogeneous particles with more than one domain of scattering density, arbitrary shape
    • Spinozzi F, Carsughi F, Mariani P, Teixeira CV, Amaral LQ. SAS from inhomogeneous particles with more than one domain of scattering density, arbitrary shape. J Appl Cryst 2000;33:556-559.
    • (2000) J Appl Cryst , vol.33 , pp. 556-559
    • Spinozzi, F.1    Carsughi, F.2    Mariani, P.3    Teixeira, C.V.4    Amaral, L.Q.5
  • 43
    • 69949132669 scopus 로고    scopus 로고
    • Crydam, from atomic coordinates of macromolecules to scattering intensity
    • Malfois M, Svergun DI. 2002. Crydam, from atomic coordinates of macromolecules to scattering intensity. See http://nobugs.dl.ac.uk/presentations/Malfois/CRYDAM.pdf.
    • (2002)
    • Malfois, M.1    Svergun, D.I.2
  • 44
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun DI, Petoukhov MV, Koch MHJ. Determination of domain structure of proteins from X-ray solution scattering. Biophys J 2001;80(6):2946-2953.
    • (2001) Biophys J , vol.80 , Issue.6 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.J.3
  • 45
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun DI. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys J 1999;2879-2886.
    • (1999) Biophys J , pp. 2879-2886
    • Svergun, D.I.1
  • 46
    • 84945101258 scopus 로고
    • New developments in direct shape determination from small-angle scattering: I
    • Svergun DI, Stuhrmann HB. New developments in direct shape determination from small-angle scattering: I. Theory and model calculations. Acta Crystallogr 1991;A47:736-744.
    • (1991) Acta Crystallogr , vol.A47 , pp. 736-744
    • Svergun, D.I.1    Stuhrmann, H.B.2
  • 47
    • 0032534405 scopus 로고    scopus 로고
    • Particle shape reconstruction by small-angle scattering: integration of group theory and maximum entropy to multipole expansion method
    • Spinozzi F, Carsughi F, Mariani, P. Particle shape reconstruction by small-angle scattering: integration of group theory and maximum entropy to multipole expansion method. J Chem Phys 1998;109:10148.
    • (1998) J Chem Phys , vol.109 , pp. 10148
    • Spinozzi, F.1    Carsughi, F.2    Mariani, P.3
  • 48
    • 12444253048 scopus 로고    scopus 로고
    • 3D structure of sulfolobus solfataricus carboxypeptidase developed by molecular modeling is confirmed by sitedirected mutagenesis and small-angle X-ray scattering
    • Occhipinti E, Martelli PL, Spinozzi F, Corsi F, Formantici C, Molteni L, Amenitsch H, Mariani P, Tortora P, Casadio R. 3D structure of sulfolobus solfataricus carboxypeptidase developed by molecular modeling is confirmed by sitedirected mutagenesis and small-angle X-ray scattering. Biophys J 2003;85:1165-1175.
    • (2003) Biophys J , vol.85 , pp. 1165-1175
    • Occhipinti, E.1    Martelli, P.L.2    Spinozzi, F.3    Corsi, F.4    Formantici, C.5    Molteni, L.6    Amenitsch, H.7    Mariani, P.8    Tortora, P.9    Casadio, R.10
  • 49
    • 0000403125 scopus 로고
    • Small-angle scattering content and error analysis
    • More PB. Small-angle scattering content and error analysis. J Appl Cryst 1980;13:168-175.
    • (1980) J Appl Cryst , vol.13 , pp. 168-175
    • More, P.B.1
  • 50
    • 0030569147 scopus 로고    scopus 로고
    • Scattering functions of semiflexible polymers with and without excluded volume effects
    • Pedersen JS, Schurtenberger P. Scattering functions of semiflexible polymers with and without excluded volume effects. Macromolecules 1996;29:7602-7612.
    • (1996) Macromolecules , vol.29 , pp. 7602-7612
    • Pedersen, J.S.1    Schurtenberger, P.2
  • 51
    • 84982060514 scopus 로고
    • Röntgenuntersuchung gelöster Fadenmolek üle
    • Kratky O, Porod G. Röntgenuntersuchung gelöster Fadenmolek üle. Rec Trav Chim Pays-Bas 1949;68:1106-1123.
    • (1949) Rec Trav Chim Pays-Bas , vol.68 , pp. 1106-1123
    • Kratky, O.1    Porod, G.2
  • 52
    • 33644606089 scopus 로고
    • Molecular-weight determination by light scattering
    • Debye P. Molecular-weight determination by light scattering. J Phys Coll Chem 1947;51:18-32.
    • (1947) J Phys Coll Chem , vol.51 , pp. 18-32
    • Debye, P.1
  • 53
    • 0034966446 scopus 로고    scopus 로고
    • Heatinduced unfolding of neocarzinostatin, a small all-beta protein investigated by small-angle X-ray scattering
    • Pérez J, Vachette P, Russo D, Desmadril M, Durand D. Heatinduced unfolding of neocarzinostatin, a small all-beta protein investigated by small-angle X-ray scattering. J Mol Biol 2001;308:721-743.
    • (2001) J Mol Biol , vol.308 , pp. 721-743
    • Pérez, J.1    Vachette, P.2    Russo, D.3    Desmadril, M.4    Durand, D.5
  • 56
    • 0037215795 scopus 로고    scopus 로고
    • Protein interactions in undersaturated and supersaturated solutions: a study using light and X-ray scattering
    • Narayanan J, Liu XY. Protein interactions in undersaturated and supersaturated solutions: a study using light and X-ray scattering. Biophys J 2003;84:523-532.
    • (2003) Biophys J , vol.84 , pp. 523-532
    • Narayanan, J.1    Liu, X.Y.2
  • 57
    • 7544220942 scopus 로고
    • Analysis of classical statistical mechanics by means of collective coordinates
    • Percus JK, Yevick GJ. Analysis of classical statistical mechanics by means of collective coordinates. Phys Rev 1958; 110:1
    • (1958) Phys Rev , vol.110 , pp. 1
    • Percus, J.K.1    Yevick, G.J.2
  • 58
    • 84933693670 scopus 로고
    • An analytic structure factor for macroion solutions
    • Hayter JB, Penfold J. An analytic structure factor for macroion solutions. Mol Phys 1981;42:109-118.
    • (1981) Mol Phys , vol.42 , pp. 109-118
    • Hayter, J.B.1    Penfold, J.2
  • 59
    • 33646110906 scopus 로고
    • A rescaled MSA structure factor for dilute charged colloidal dispersions
    • Hansen JP, Hayter JB. A rescaled MSA structure factor for dilute charged colloidal dispersions. Mol Phys 1982;46:651-656.
    • (1982) Mol Phys , vol.46 , pp. 651-656
    • Hansen, J.P.1    Hayter, J.B.2
  • 60
    • 0026927061 scopus 로고
    • Colloidal dispersions: use of exact potentials approximation
    • Kelkar VK, Narayanan J, Manohar C. Colloidal dispersions: use of exact potentials approximation. Langmuir 1992;8:2210-2214.
    • (1992) Langmuir , vol.8 , pp. 2210-2214
    • Kelkar, V.K.1    Narayanan, J.2    Manohar, C.3
  • 61
    • 0031768735 scopus 로고    scopus 로고
    • Protein interactions in solution characterized by light and neutron scattering: comparison of lysozyme and chymotrypsinogen
    • Velev OD, Kaler EW, Lenhoff AM. Protein interactions in solution characterized by light and neutron scattering: comparison of lysozyme and chymotrypsinogen. Biophys J 1997;75:2682-2697.
    • (1997) Biophys J , vol.75 , pp. 2682-2697
    • Velev, O.D.1    Kaler, E.W.2    Lenhoff, A.M.3
  • 62
    • 0032484699 scopus 로고    scopus 로고
    • Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes
    • Curtis RA, Prausnitz JM, Blanch HW. Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes. Biotechnol Bioeng 1998;57:11-21.
    • (1998) Biotechnol Bioeng , vol.57 , pp. 11-21
    • Curtis, R.A.1    Prausnitz, J.M.2    Blanch, H.W.3
  • 64
    • 0003626648 scopus 로고
    • All About Albumin
    • New York: Academic Press
    • Peters TJr. All About Albumin. New York: Academic Press; 1995.
    • (1995)
    • Peters Jr., T.1
  • 65
    • 20444414123 scopus 로고    scopus 로고
    • Small angle X-ray scattering on solutions of carboxymethyl cellulose and bovine serum albumin
    • Pancera SM, Itri R, Petri DF. Small angle X-ray scattering on solutions of carboxymethyl cellulose and bovine serum albumin. Macromol Biosci 2005;5:331-336
    • (2005) Macromol Biosci , vol.5 , pp. 331
    • Pancera, S.M.1    Itri, R.2    Petri, D.F.3
  • 66
    • 69249089296 scopus 로고    scopus 로고
    • Polyelectrolyte protein complexation driven by charge regulation
    • Silva FLB, Jonsson B. Polyelectrolyte protein complexation driven by charge regulation. Soft Matter 2009;5:2862-2868.
    • (2009) Soft Matter , vol.5 , pp. 2862-2868
    • Silva, F.L.B.1    Jonsson, B.2
  • 67
    • 11744320872 scopus 로고
    • The viscosity of aqueous solutions of bovine serum albumin between pH 4
    • Tanford C, Buzzel JG. The viscosity of aqueous solutions of bovine serum albumin between pH 4.3 and 10.5. J Phys Chem 1956;60:225-231.
    • (1956) J Phys Chem , vol.60 , pp. 225-231
    • Tanford, C.1    Buzzel, J.G.2
  • 68
    • 0003101421 scopus 로고
    • Takeda, reformation of the helical structure of bovine serum albumin by the addition of small amounts of sodium dodecyl sulfate after the disruption of the structure by urea
    • Moriyama Y, Sato K. Takeda, reformation of the helical structure of bovine serum albumin by the addition of small amounts of sodium dodecyl sulfate after the disruption of the structure by urea. J Coll Interf Sci 1993;156:420.
    • (1993) J Coll Interf Sci , vol.156 , pp. 420
    • Moriyama, Y.1    Sato, K.2
  • 69
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • Carter DC, Ho JX. Structure of serum albumin. Adv Protein Chem 1994;45:153-203.
    • (1994) Adv Protein Chem , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 70
    • 0028558671 scopus 로고
    • Preliminary crystallographic studies of four crystal forms of serum albumin
    • Carter D, Chang B, Ho JX, Keeling K, Krishnasami Z. Preliminary crystallographic studies of four crystal forms of serum albumin. Eur J Biochem 1994;226:1049-1052.
    • (1994) Eur J Biochem , vol.226 , pp. 1049-1052
    • Carter, D.1    Chang, B.2    Ho, J.X.3    Keeling, K.4    Krishnasami, Z.5
  • 71
    • 0035041251 scopus 로고    scopus 로고
    • The conformation of serum albumin in solution: a combined phosphorescence depolarization-hydrodynamic modeling study
    • Ferrer ML, Duchowicz R, Carrasco B, De La Torre JG, Acunũa AU. The conformation of serum albumin in solution: a combined phosphorescence depolarization-hydrodynamic modeling study. Biophys J 2001;80:2422-2430.
    • (2001) Biophys J , vol.80 , pp. 2422-2430
    • Ferrer, M.L.1    Duchowicz, R.2    Carrasco, B.3    De La Torre, J.G.4    Acunũa, A.U.5
  • 72
    • 0034287494 scopus 로고    scopus 로고
    • Spectroscopic studies on the interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants
    • Part A
    • Gelamo EL, Tabak M. Spectroscopic studies on the interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants. Spectrochim Acta 2000;56(Part A):2255.
    • (2000) Spectrochim Acta , vol.56 , pp. 2255
    • Gelamo, E.L.1    Tabak, M.2
  • 73
    • 65249157372 scopus 로고    scopus 로고
    • Stable intermediates determine proteins' primary unfolding sites in the presence of surfactants
    • Hansen JH, Petersen SV, Andersen KK, Damhus JJET, Otzen D. Stable intermediates determine proteins' primary unfolding sites in the presence of surfactants. Biopolymers 2008;91:221.
    • (2008) Biopolymers , vol.91 , pp. 221
    • Hansen, J.H.1    Petersen, S.V.2    Andersen, K.K.3    Damhus, J.J.E.T.4    Otzen, D.5
  • 74
    • 4043159165 scopus 로고    scopus 로고
    • Bovine serum albumin (BSA) plays a role in the size of SDS micelle-like aggregates at the saturation binding: the ionic strength effect
    • Shweitzer B, Zanette D, Itri R. Bovine serum albumin (BSA) plays a role in the size of SDS micelle-like aggregates at the saturation binding: the ionic strength effect. J Coll Interf Sci 2004;277:285-291.
    • (2004) J Coll Interf Sci , vol.277 , pp. 285-291
    • Shweitzer, B.1    Zanette, D.2    Itri, R.3
  • 75
    • 33751155438 scopus 로고
    • Spectroscopic probe analysis of protein-surfactant interactions: the BSA/SDS system
    • Turro NJ, Ananthapadmanabhan KP, Lei XG, Aronson M. Spectroscopic probe analysis of protein-surfactant interactions: the BSA/SDS system. Langmuir 1995;11:2525.
    • (1995) Langmuir , vol.11 , pp. 2525
    • Turro, N.J.1    Ananthapadmanabhan, K.P.2    Lei, X.G.3    Aronson, M.4
  • 76
    • 0000442621 scopus 로고
    • Structure and fractal dimension of protein-detergent complexes
    • Chen SH, Teixeira J. Structure and fractal dimension of protein-detergent complexes. Phys Rev Lett 1986;57:2583-2586.
    • (1986) Phys Rev Lett , vol.57 , pp. 2583-2586
    • Chen, S.H.1    Teixeira, J.2
  • 77
    • 0025091757 scopus 로고
    • Small-angle neutron scattering study of the structure of protein/detergent complexes
    • Guo XH, Zhao NM, Chen SH, Teixeira J. Small-angle neutron scattering study of the structure of protein/detergent complexes. Biopolymers 1990;29;335.
    • (1990) Biopolymers , vol.29 , pp. 335
    • Guo, X.H.1    Zhao, N.M.2    Chen, S.H.3    Teixeira, J.4
  • 78
    • 0000240071 scopus 로고
    • Micellar-shape anisometry near isotropic-liquid-crystal phase transitions
    • Itri R, Amaral LQ. Micellar-shape anisometry near isotropic-liquid-crystal phase transitions. Phys Rev E 1993;47:2551.
    • (1993) Phys Rev E , vol.47 , pp. 2551
    • Itri, R.1    Amaral, L.Q.2
  • 79
    • 33845375574 scopus 로고
    • Effect of pentanol and concentration on the micelles in the system OBS/water/n-pentanol
    • Marignan J, Basserau P, Delord P. Effect of pentanol and concentration on the micelles in the system OBS/water/n-pentanol. J Phys Chem 1986;90:645-52.
    • (1986) J Phys Chem , vol.90 , pp. 645-652
    • Marignan, J.1    Basserau, P.2    Delord, P.3
  • 81
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe DJ. Folding proteins in fatal ways. Nature 2003;426:900-904.
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.