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Volumn 96, Issue 1, 2009, Pages 169-179

Equilibrium unfolding thermodynamics of β2-microglobulin analyzed through native-state H/D exchange

Author keywords

[No Author keywords available]

Indexed keywords

BETA 2 MICROGLOBULIN; HYDROGEN; RECOMBINANT PROTEIN; WATER;

EID: 58849151382     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.108.142448     Document Type: Article
Times cited : (20)

References (49)
  • 2
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • Englander, S. W., and N. R. Kallenbach. 1984. Hydrogen exchange and structural dynamics of proteins and nucleic acids. Q. Rev. Biophys. 16:521-655.
    • (1984) Q. Rev. Biophys , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 3
    • 0030580089 scopus 로고    scopus 로고
    • Structure-based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors
    • Hilser, V. J., and E. Freire. 1996. Structure-based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors. J. Mol. Biol. 262:756-772.
    • (1996) J. Mol. Biol , vol.262 , pp. 756-772
    • Hilser, V.J.1    Freire, E.2
  • 4
    • 0022391603 scopus 로고
    • A new form of amyloid protein associated with chronic hemodialysis was identified as β2-microglobulin
    • Gejyo, F., T. Yamada, S. Odani, Y. Nakagawa, M. Arakawa, et al. 1985. A new form of amyloid protein associated with chronic hemodialysis was identified as β2-microglobulin. Biochem. Biophys. Res. Commun. 129:701-706.
    • (1985) Biochem. Biophys. Res. Commun , vol.129 , pp. 701-706
    • Gejyo, F.1    Yamada, T.2    Odani, S.3    Nakagawa, Y.4    Arakawa, M.5
  • 5
    • 0013994339 scopus 로고    scopus 로고
    • Hydrogen exchange in proteins
    • Hvidt, A., and S. O. Nielsen. 1996. Hydrogen exchange in proteins. Adv. Protein Chem. 21:287-386.
    • (1996) Adv. Protein Chem , vol.21 , pp. 287-386
    • Hvidt, A.1    Nielsen, S.O.2
  • 6
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai, Y.,J.S.Milne,L. Mayne, and S. W. Englander. 1993. Primary structure effects on peptide group hydrogen exchange. Proteins. 17:75-86.
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 8
    • 0030047378 scopus 로고    scopus 로고
    • Temperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domain
    • Swint-Kruse, L., and A. D. Robertson. 1996. Temperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domain. Biochemistry. 35:171-180.
    • (1996) Biochemistry , vol.35 , pp. 171-180
    • Swint-Kruse, L.1    Robertson, A.D.2
  • 9
    • 0029872925 scopus 로고    scopus 로고
    • A general two-process model describes the hydrogen exchange behavior of RNase A in unfolding conditions
    • Loh, S. N., C. A. Rohl, T. Kiefhaber, and R. L. Baldwin. 1996. A general two-process model describes the hydrogen exchange behavior of RNase A in unfolding conditions. Proc. Natl. Acad. Sci. USA. 93:1982-1987.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1982-1987
    • Loh, S.N.1    Rohl, C.A.2    Kiefhaber, T.3    Baldwin, R.L.4
  • 10
    • 18244412979 scopus 로고    scopus 로고
    • Removal of the N-terminal hexapeptide from human β2-micro-globulin facilitates protein aggregation and fibril formation
    • Esposito, G., R. Michelutti, G. Verdone, P. Viglino, H. Hernández, et al. 2000. Removal of the N-terminal hexapeptide from human β2-micro-globulin facilitates protein aggregation and fibril formation. Protein Sci. 9:831-845.
    • (2000) Protein Sci , vol.9 , pp. 831-845
    • Esposito, G.1    Michelutti, R.2    Verdone, G.3    Viglino, P.4    Hernández, H.5
  • 11
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen, G., and D. J. Ruben. 1980. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Lett. 69:185-189.
    • (1980) Chem. Phys. Lett , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 12
    • 13444269041 scopus 로고
    • Computer-optimized decoupling scheme for wideband applications and low-level operation
    • Shaka, A. J., P. B. Barker, and R. Freeman. 1985. Computer-optimized decoupling scheme for wideband applications and low-level operation. J. Magn. Reson. 64:547-552.
    • (1985) J. Magn. Reson , vol.64 , pp. 547-552
    • Shaka, A.J.1    Barker, P.B.2    Freeman, R.3
  • 14
    • 0033686354 scopus 로고    scopus 로고
    • Kinetic constant measurement by NMR using a calibrated internal signal ERETIC
    • Billault, I., and S. Akoka. 2000. Kinetic constant measurement by NMR using a calibrated internal signal ERETIC. Instrum. Sci. Technol. 28:233-240.
    • (2000) Instrum. Sci. Technol , vol.28 , pp. 233-240
    • Billault, I.1    Akoka, S.2
  • 15
    • 1842783110 scopus 로고    scopus 로고
    • The application of the ERETIC method to 2D-NMR
    • Michel, N., and S. Akoka. 2004. The application of the ERETIC method to 2D-NMR. J. Magn. Reson. 168:118-123.
    • (2004) J. Magn. Reson , vol.168 , pp. 118-123
    • Michel, N.1    Akoka, S.2
  • 17
    • 0019076960 scopus 로고
    • Hydrogen isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor
    • Woodward, C. K., and B. D. Hilton. 1980. Hydrogen isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor. Biophys. J. 32:561-575.
    • (1980) Biophys. J , vol.32 , pp. 561-575
    • Woodward, C.K.1    Hilton, B.D.2
  • 18
    • 0037214137 scopus 로고    scopus 로고
    • Protein hydrogen exchange mechanism: Local fluctuations
    • Maity, H., K. L. Woon, J. N. Rumbley, and S. W. Englander. 2003. Protein hydrogen exchange mechanism: local fluctuations. Protein Sci. 12:153-160.
    • (2003) Protein Sci , vol.12 , pp. 153-160
    • Maity, H.1    Woon, K.L.2    Rumbley, J.N.3    Englander, S.W.4
  • 19
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai, Y., T. R. Sosnick, L. Mayne, and S. W. Englander. 1995. Protein folding intermediates: native-state hydrogen exchange. Science. 269:192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 20
    • 0027977883 scopus 로고
    • Protein hydrogen exchange in denaturant: Quantitative analysis by a two-process model
    • Qian, H., S. L. Mayo, and A. Morton. 1994. Protein hydrogen exchange in denaturant: quantitative analysis by a two-process model. Biochemistry. 33:8167-8171.
    • (1994) Biochemistry , vol.33 , pp. 8167-8171
    • Qian, H.1    Mayo, S.L.2    Morton, A.3
  • 21
    • 0031582071 scopus 로고    scopus 로고
    • Thermodynamic hierarchy and local energetics of folded proteins
    • Qian, H. 1997. Thermodynamic hierarchy and local energetics of folded proteins. J. Mol. Biol. 267:198-206.
    • (1997) J. Mol. Biol , vol.267 , pp. 198-206
    • Qian, H.1
  • 22
    • 0033582788 scopus 로고    scopus 로고
    • Hydrogen exchange kinetics of proteins in denaturants: A generalized two-process model
    • Qian, H., and S. I. Chan. 1999. Hydrogen exchange kinetics of proteins in denaturants: a generalized two-process model. J. Mol. Biol. 286:607-616.
    • (1999) J. Mol. Biol , vol.286 , pp. 607-616
    • Qian, H.1    Chan, S.I.2
  • 23
    • 0035896018 scopus 로고    scopus 로고
    • Detection of two partially structured species in the folding process of the amyloidogenic protein β2-microglobulin
    • Chiti, F., P. Mangione, A. Andreola, S. Giorgetti, M. Stefani, et al. 2001. Detection of two partially structured species in the folding process of the amyloidogenic protein β2-microglobulin. J. Mol. Biol. 307:379-391.
    • (2001) J. Mol. Biol , vol.307 , pp. 379-391
    • Chiti, F.1    Mangione, P.2    Andreola, A.3    Giorgetti, S.4    Stefani, M.5
  • 24
    • 10744219788 scopus 로고    scopus 로고
    • Properties of some variants of human β2-microglobulin and amyloidogenesis
    • Corazza, A., F. Pettirossi, P. Viglino, G. Verdone, J. Garcia, et al. 2004. Properties of some variants of human β2-microglobulin and amyloidogenesis. J. Biol. Chem. 279:9176-9189.
    • (2004) J. Biol. Chem , vol.279 , pp. 9176-9189
    • Corazza, A.1    Pettirossi, F.2    Viglino, P.3    Verdone, G.4    Garcia, J.5
  • 25
  • 26
    • 0026342150 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding
    • Jackson, S. E., and A. R. Fersht. 1991. Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding. Biochemistry. 30:10436-10443.
    • (1991) Biochemistry , vol.30 , pp. 10436-10443
    • Jackson, S.E.1    Fersht, A.R.2
  • 27
    • 34547275473 scopus 로고
    • Brownian motion in a field of force and the diffusion model of chemical reactions
    • Kramers, H. A. 1940. Brownian motion in a field of force and the diffusion model of chemical reactions. Physica (Utrecht). 7:284-304.
    • (1940) Physica (Utrecht) , vol.7 , pp. 284-304
    • Kramers, H.A.1
  • 28
    • 11244309572 scopus 로고    scopus 로고
    • Direct measurement of the thermodynamic parameters of amyloid formation by isothermal titration calorimetry
    • Kardos, J., K. Yamamoto, K. Hasegawa, H. Naiki, and Y. Goto. 2004. Direct measurement of the thermodynamic parameters of amyloid formation by isothermal titration calorimetry. J. Biol. Chem. 279:55308-55314.
    • (2004) J. Biol. Chem , vol.279 , pp. 55308-55314
    • Kardos, J.1    Yamamoto, K.2    Hasegawa, K.3    Naiki, H.4    Goto, Y.5
  • 29
    • 0032766705 scopus 로고    scopus 로고
    • Experimental study of the protein folding landscape: Unfolding reactions in cytochrome c
    • Milne, J. S., Y. Xu, L. C. Mayne, and S. W. Englander. 1999. Experimental study of the protein folding landscape: unfolding reactions in cytochrome c. J. Mol. Biol. 290:811-822.
    • (1999) J. Mol. Biol , vol.290 , pp. 811-822
    • Milne, J.S.1    Xu, Y.2    Mayne, L.C.3    Englander, S.W.4
  • 30
    • 0034635173 scopus 로고    scopus 로고
    • Comparisons of pressure and temperature activation parameters for amide hydrogen exchange in T4 lysozyme
    • Dixon, M. E., T. K. Hitchens, and R. G. Bryant. 2000. Comparisons of pressure and temperature activation parameters for amide hydrogen exchange in T4 lysozyme. Biochemistry. 39:248-254.
    • (2000) Biochemistry , vol.39 , pp. 248-254
    • Dixon, M.E.1    Hitchens, T.K.2    Bryant, R.G.3
  • 31
    • 0014722597 scopus 로고
    • Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: A ubiquitous property of water
    • Lumry, R., and S. Rajender. 1970. Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: a ubiquitous property of water. Biopolymers. 9:1125-1227.
    • (1970) Biopolymers , vol.9 , pp. 1125-1227
    • Lumry, R.1    Rajender, S.2
  • 32
    • 33847798713 scopus 로고
    • Enthalpy-entropy compensation. 1. Some fundamental statistical problems associated with the analysis of van't Hoff and Arrhenius data
    • Krug,R., W. Hunter, and R. Grieger. 1976. Enthalpy-entropy compensation. 1. Some fundamental statistical problems associated with the analysis of van't Hoff and Arrhenius data. J. Phys. Chem. 80:2335-2341.
    • (1976) J. Phys. Chem , vol.80 , pp. 2335-2341
    • Krug, R.1    Hunter, W.2    Grieger, R.3
  • 33
    • 33847798413 scopus 로고
    • Enthalpy-entropy compensation. 2. Separation of the chemical from the statistical effect
    • Krug, R., W. Hunter, and R. Grieger. 1976. Enthalpy-entropy compensation. 2. Separation of the chemical from the statistical effect. J. Phys. Chem. 80:2341-2351.
    • (1976) J. Phys. Chem , vol.80 , pp. 2341-2351
    • Krug, R.1    Hunter, W.2    Grieger, R.3
  • 34
    • 0000525863 scopus 로고
    • Solvent reorganization and thermodynamic enthalpy-entropy compensation
    • Grunwald, E., and C. Steel. 1995. Solvent reorganization and thermodynamic enthalpy-entropy compensation. J. Am. Chem. Soc. 117:5687-5692.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 5687-5692
    • Grunwald, E.1    Steel, C.2
  • 35
    • 0029395478 scopus 로고
    • Win some, lose some: Enthalpy-entropy compensation in weak intermolecular interactions
    • Dunitz, J. D. 1995. Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactions. Chem. Biol. 2:709-712.
    • (1995) Chem. Biol , vol.2 , pp. 709-712
    • Dunitz, J.D.1
  • 36
    • 33645831413 scopus 로고    scopus 로고
    • Entropy-enthalpy compensation: Perturbation and relaxation in thermodynamic systems
    • Qian, H., and J. J. Hopfield. 1996. Entropy-enthalpy compensation: perturbation and relaxation in thermodynamic systems. J. Chem. Phys. 105:9292-9299.
    • (1996) J. Chem. Phys , vol.105 , pp. 9292-9299
    • Qian, H.1    Hopfield, J.J.2
  • 37
    • 0000592009 scopus 로고    scopus 로고
    • Successful predictions of the residual motion of weakly associated species as a function of the bonding between them
    • Westwell, M. S., M. S. Searle, J. Klein, and D. H. Williams. 1996. Successful predictions of the residual motion of weakly associated species as a function of the bonding between them. J. Phys. Chem. 100:16000-16001.
    • (1996) J. Phys. Chem , vol.100 , pp. 16000-16001
    • Westwell, M.S.1    Searle, M.S.2    Klein, J.3    Williams, D.H.4
  • 38
    • 0034658244 scopus 로고    scopus 로고
    • A study on the enthalpy-entropy compensation in protein unfolding
    • Liu, L., C. Yang, and Q. X. Guo. 2000. A study on the enthalpy-entropy compensation in protein unfolding. Biophys. Chem. 84:239-251.
    • (2000) Biophys. Chem , vol.84 , pp. 239-251
    • Liu, L.1    Yang, C.2    Guo, Q.X.3
  • 39
    • 0035107447 scopus 로고    scopus 로고
    • Entropy-enthalpy compensation: Fact or artifact?
    • Sharp, K. 2001. Entropy-enthalpy compensation: fact or artifact? Protein Sci. 10:661-667.
    • (2001) Protein Sci , vol.10 , pp. 661-667
    • Sharp, K.1
  • 40
    • 0035965868 scopus 로고    scopus 로고
    • Heat does not come in different colours: Entropy-enthalpy compensation, free energy windows, quantum confinement, pressure perturbation calorimetry, solvation and the multiple causes of heat capacity effects in biomolecular interactions
    • Cooper, A., C. M. Johnson, J. H. Lakey, and M. Nöllmann. 2001. Heat does not come in different colours: entropy-enthalpy compensation, free energy windows, quantum confinement, pressure perturbation calorimetry, solvation and the multiple causes of heat capacity effects in biomolecular interactions. Biophys. Chem. 93:215-230.
    • (2001) Biophys. Chem , vol.93 , pp. 215-230
    • Cooper, A.1    Johnson, C.M.2    Lakey, J.H.3    Nöllmann, M.4
  • 41
    • 33745224979 scopus 로고    scopus 로고
    • Collagen plays an active role in the aggregation of β2-microglo-bulin under physiopathological conditions of dialysis-related amyloidosis
    • Relini, A., C. Canale, S. De Stefano, R. Rolandi, S. Giorgetti, et al. 2006. Collagen plays an active role in the aggregation of β2-microglo-bulin under physiopathological conditions of dialysis-related amyloidosis. J. Biol. Chem. 281:16521-16529.
    • (2006) J. Biol. Chem , vol.281 , pp. 16521-16529
    • Relini, A.1    Canale, C.2    De Stefano, S.3    Rolandi, R.4    Giorgetti, S.5
  • 42
    • 18244378561 scopus 로고    scopus 로고
    • The solution structure of human β2-microglobulin reveals the prodromes of its amyloid transition
    • Verdone, G., A. Corazza, P. Viglino, F. Pettirossi, S. Giorgetti, et al. 2002. The solution structure of human β2-microglobulin reveals the prodromes of its amyloid transition. Protein Sci. 11:487-499.
    • (2002) Protein Sci , vol.11 , pp. 487-499
    • Verdone, G.1    Corazza, A.2    Viglino, P.3    Pettirossi, F.4    Giorgetti, S.5
  • 43
    • 0037162520 scopus 로고    scopus 로고
    • Crystal structure of monomeric human β-2-microglobulin reveals clues to its amyloidogenic properties
    • Trinh, C. H., D. P. Smith, A. P. Kalverda, S. E. V. Phillips, and S. E. Radford. 2002. Crystal structure of monomeric human β-2-microglobulin reveals clues to its amyloidogenic properties. Proc. Natl. Acad. Sci. USA. 99:9771-9776.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9771-9776
    • Trinh, C.H.1    Smith, D.P.2    Kalverda, A.P.3    Phillips, S.E.V.4    Radford, S.E.5
  • 44
    • 36849083472 scopus 로고    scopus 로고
    • High-resolution crystal structure of β2-microglobulin formed at pH 7.0
    • Iwata, K., T. Matsuura, K. Sakurai, A. Nakagawa, and Y. Goto. 2007. High-resolution crystal structure of β2-microglobulin formed at pH 7.0. J. Biochem. 142:413-419.
    • (2007) J. Biochem , vol.142 , pp. 413-419
    • Iwata, K.1    Matsuura, T.2    Sakurai, K.3    Nakagawa, A.4    Goto, Y.5
  • 46
    • 0023176346 scopus 로고
    • Structure of the human class I histocompatibility antigen, HLA-A2
    • Bjorkman, P. J., M. A. Saper, B. Samaroui, W. S. Bennet, J. L. Strominger, et al. 1987. Structure of the human class I histocompatibility antigen, HLA-A2. Nature. 329:506-512.
    • (1987) Nature , vol.329 , pp. 506-512
    • Bjorkman, P.J.1    Saper, M.A.2    Samaroui, B.3    Bennet, W.S.4    Strominger, J.L.5
  • 48
    • 0036708005 scopus 로고    scopus 로고
    • The role of disulfide bond in the amyloidogenic state of β2-microglobulin studied by heteronuclear NMR
    • Katou, H., T. Kanno, M. Hoshino, Y. Hagihara, H. Tanaka, et al. 2002. The role of disulfide bond in the amyloidogenic state of β2-microglobulin studied by heteronuclear NMR. Protein Sci. 11:2218-2229.
    • (2002) Protein Sci , vol.11 , pp. 2218-2229
    • Katou, H.1    Kanno, T.2    Hoshino, M.3    Hagihara, Y.4    Tanaka, H.5
  • 49
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., M. Billeter, and K. Wüthrich. 1996. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:51-55.
    • (1996) J. Mol. Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3


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