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Volumn 51, Issue 23, 2012, Pages 4723-4734

Four-state folding of a SH3 domain: Salt-induced modulation of the stabilities of the intermediates and native state

Author keywords

[No Author keywords available]

Indexed keywords

CHEVRON PLOT; FOLDING PATHWAY; GUANIDINE HYDROCHLORIDE; HOFMEISTER EFFECTS; KINETIC DATA; MOLTEN GLOBULE; NATIVE STATE; PI3-KINASE; RATE LIMITING; RATE-LIMITING STEPS; STRUCTURAL COMPONENT;

EID: 84862162074     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300223b     Document Type: Article
Times cited : (16)

References (102)
  • 1
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • Jackson, S. E. (1998) How do small single-domain proteins fold? Folding Des. 3, R81-R91
    • (1998) Folding Des. , vol.3
    • Jackson, S.E.1
  • 2
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • DOI 10.1006/jmbi.1998.1645
    • Plaxco, K. W., Simons, K. T., and Baker, D. (1998) Contact order, transition state placement and the refolding rates of single domain proteins J. Mol. Biol. 277, 985-994 (Pubitemid 28195995)
    • (1998) Journal of Molecular Biology , vol.277 , Issue.4 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 3
    • 0036678120 scopus 로고    scopus 로고
    • Experimental evaluation of topological parameters determining protein-folding rates
    • Miller, E. J., Fischer, K. F., and Marqusee, S. (2002) Experimental evaluation of topological parameters determining protein-folding rates Proc. Natl. Acad. Sci. U.S.A. 99, 10359-10363
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 10359-10363
    • Miller, E.J.1    Fischer, K.F.2    Marqusee, S.3
  • 4
    • 18344371857 scopus 로고    scopus 로고
    • A statistical model for predicting protein folding rates from amino acid sequence with structural class information
    • DOI 10.1021/ci049757q
    • Gromiha, M. M. (2005) A statistical model for predicting protein folding rates from amino acid sequence with structural class information J. Chem. Inf. Model. 45, 494-501 (Pubitemid 40635357)
    • (2005) Journal of Chemical Information and Modeling , vol.45 , Issue.2 , pp. 494-501
    • Gromiha, M.M.1
  • 5
    • 42749106226 scopus 로고    scopus 로고
    • Finite size effects on thermal denaturation of globular proteins
    • Li, M. S., Klimov, D. K., and Thirumalai, D. (2004) Finite size effects on thermal denaturation of globular proteins Phys. Rev. Lett. 93, 268107
    • (2004) Phys. Rev. Lett. , vol.93 , pp. 268107
    • Li, M.S.1    Klimov, D.K.2    Thirumalai, D.3
  • 7
    • 0035173844 scopus 로고    scopus 로고
    • The roles of stability and contact order in determining protein folding rates
    • DOI 10.1038/83003
    • Dinner, A. R. and Karplus, M. (2001) The roles of stability and contact order in determining protein folding rates Nat. Struct. Biol. 8, 21-22 (Pubitemid 32043021)
    • (2001) Nature Structural Biology , vol.8 , Issue.1 , pp. 21-22
    • Dinner, A.R.1    Karplus, M.2
  • 8
    • 0028958601 scopus 로고
    • Characterizing transition states in protein folding: An essential step in the puzzle
    • Fersht, A. R. (1995) Characterizing transition states in protein folding: An essential step in the puzzle Curr. Opin. Struct. Biol. 5, 79-84
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 79-84
    • Fersht, A.R.1
  • 9
    • 84859444101 scopus 로고    scopus 로고
    • A residue in helical conformation in the native state adopts a β-strand conformation in the folding transition state despite its high and canonical φ-value
    • Zarrine-Afsar, A., Dahesh, S., and Davidson, A. R. (2012) A residue in helical conformation in the native state adopts a β-strand conformation in the folding transition state despite its high and canonical φ-value Proteins 80, 1343-1349
    • (2012) Proteins , vol.80 , pp. 1343-1349
    • Zarrine-Afsar, A.1    Dahesh, S.2    Davidson, A.R.3
  • 10
    • 0034112774 scopus 로고    scopus 로고
    • Kinetics, thermodynamics and evolution of non-native interactions in a protein folding nucleus
    • DOI 10.1038/74111
    • Li, L., Mirny, L. A., and Shakhnovich, E. I. (2000) Kinetics, thermodynamics and evolution of non-native interactions in a protein folding nucleus Nat. Struct. Biol. 7, 336-342 (Pubitemid 30194459)
    • (2000) Nature Structural Biology , vol.7 , Issue.4 , pp. 336-342
    • Li, L.1    Mirny, L.A.2    Shakhnovich, E.I.3
  • 11
    • 0036295960 scopus 로고    scopus 로고
    • Stiffness of the distal loop restricts the structural heterogeneity of the transition state ensemble in SH3 domains
    • DOI 10.1006/jmbi.2002.5453
    • Klimov, D. K. and Thirumalai, D. (2002) Stiffness of the distal loop restricts the structural heterogeneity of the transition state ensemble in SH3 domains J. Mol. Biol. 317, 721-737 (Pubitemid 34722160)
    • (2002) Journal of Molecular Biology , vol.317 , Issue.5 , pp. 721-737
    • Klimov, D.K.1    Thirumalai, D.2
  • 12
    • 24044551638 scopus 로고    scopus 로고
    • Transition state contact orders correlate with protein folding rates
    • DOI 10.1016/j.jmb.2005.06.081, PII S0022283605008065
    • Paci, E., Lindorff-Larsen, K., Dobson, C. M., Karplus, M., and Vendruscolo, M. (2005) Transition state contact orders correlate with protein folding rates J. Mol. Biol. 352, 495-500 (Pubitemid 41225462)
    • (2005) Journal of Molecular Biology , vol.352 , Issue.3 , pp. 495-500
    • Paci, E.1    Lindorff-Larsen, K.2    Dobson, C.M.3    Karplus, M.4    Vendruscolo, M.5
  • 13
    • 0020972782 scopus 로고
    • Theoretical studies of protein folding
    • Go, N. (1983) Theoretical studies of protein folding Annu. Rev. Biophys. Bioeng. 12, 183-210
    • (1983) Annu. Rev. Biophys. Bioeng. , vol.12 , pp. 183-210
    • Go, N.1
  • 15
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson, J. D., Onuchic, J. N., Socci, N. D., and Wolynes, P. G. (1995) Funnels, pathways, and the energy landscape of protein folding: A synthesis Proteins 21, 167-195
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 18
    • 1542358783 scopus 로고    scopus 로고
    • Increasing Stability Reduces Conformational Heterogeneity in a Protein Folding Intermediate Ensemble
    • DOI 10.1016/j.jmb.2003.12.083, PII S0022283604000853
    • Sridevi, K., Lakshmikanth, G. S., Krishnamoorthy, G., and Udgaonkar, J. B. (2004) Increasing stability reduces conformational heterogeneity in a protein folding intermediate ensemble J. Mol. Biol. 337, 699-711 (Pubitemid 38326885)
    • (2004) Journal of Molecular Biology , vol.337 , Issue.3 , pp. 699-711
    • Sridevi, K.1    Lakshmikanth, G.S.2    Krishnamoorthy, G.3    Udgaonkar, J.B.4
  • 19
    • 67651087326 scopus 로고    scopus 로고
    • Continuous dissolution of structure during the unfolding of a small protein
    • Jha, S. K., Dhar, D., Krishnamoorthy, G., and Udgaonkar, J. B. (2009) Continuous dissolution of structure during the unfolding of a small protein Proc. Natl. Acad. Sci. U.S.A. 106, 11113-11118
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 11113-11118
    • Jha, S.K.1    Dhar, D.2    Krishnamoorthy, G.3    Udgaonkar, J.B.4
  • 20
    • 73949098098 scopus 로고    scopus 로고
    • Native state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration
    • Wani, A. H. and Udgaonkar, J. B. (2009) Native state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration Proc. Natl. Acad. Sci. U.S.A. 106, 20711-20716
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 20711-20716
    • Wani, A.H.1    Udgaonkar, J.B.2
  • 21
    • 0028901085 scopus 로고
    • The folding mechanism of barstar: Evidence for multiple pathways and multiple intermediates
    • Shastry, M. C. and Udgaonkar, J. B. (1995) The folding mechanism of barstar: Evidence for multiple pathways and multiple intermediates J. Mol. Biol. 247, 1013-1027
    • (1995) J. Mol. Biol. , vol.247 , pp. 1013-1027
    • Shastry, M.C.1    Udgaonkar, J.B.2
  • 22
    • 0033551522 scopus 로고    scopus 로고
    • Observation of multistate kinetics during the slow folding and unfolding of barstar
    • Bhuyan, A. K. and Udgaonkar, J. B. (1999) Observation of multistate kinetics during the slow folding and unfolding of barstar Biochemistry 38, 9158-9168
    • (1999) Biochemistry , vol.38 , pp. 9158-9168
    • Bhuyan, A.K.1    Udgaonkar, J.B.2
  • 23
    • 35448932093 scopus 로고    scopus 로고
    • Characterization of the folding and unfolding reactions of single-chain monellin: Evidence for multiple intermediates and competing pathways
    • DOI 10.1021/bi701142a
    • Patra, A. K. and Udgaonkar, J. B. (2007) Characterization of the folding and unfolding reactions of single-chain monellin: Evidence for multiple intermediates and competing pathways Biochemistry 46, 11727-11743 (Pubitemid 47623741)
    • (2007) Biochemistry , vol.46 , Issue.42 , pp. 11727-11743
    • Patra, A.K.1    Udgaonkar, J.B.2
  • 24
    • 48249140760 scopus 로고    scopus 로고
    • Multiple routes and structural heterogeneity in protein folding
    • Udgaonkar, J. B. (2008) Multiple routes and structural heterogeneity in protein folding Annu. Rev. Biophys. 37, 489-510
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 489-510
    • Udgaonkar, J.B.1
  • 25
    • 79953906735 scopus 로고    scopus 로고
    • Identification of multiple folding pathways of monellin using pulsed thiol labeling and mass spectrometry
    • Jha, S. K., Dasgupta, A., Malhotra, P., and Udgaonkar, J. B. (2011) Identification of multiple folding pathways of monellin using pulsed thiol labeling and mass spectrometry Biochemistry 50, 3062-3074
    • (2011) Biochemistry , vol.50 , pp. 3062-3074
    • Jha, S.K.1    Dasgupta, A.2    Malhotra, P.3    Udgaonkar, J.B.4
  • 26
    • 0037073934 scopus 로고    scopus 로고
    • Experimental identification of downhill protein folding
    • DOI 10.1126/science.1077809
    • Garcia-Mira, M. M., Sadqi, M., Fischer, N., Sanchez-Ruiz, J. M., and Munoz, V. (2002) Experimental identification of downhill protein folding Science 298, 2191-2195 (Pubitemid 35471244)
    • (2002) Science , vol.298 , Issue.5601 , pp. 2191-2195
    • Garcia-Mira, M.M.1    Sadqi, M.2    Fischer, N.3    Sanchez-Ruiz, J.M.4    Munoz, V.5
  • 27
    • 23944522022 scopus 로고    scopus 로고
    • Downhill protein folding: Evolution meets physics
    • DOI 10.1016/j.crvi.2005.02.007, PII S1631069105000326
    • Gruebele, M. (2005) Downhill protein folding: Evolution meets physics C. R. Biol. 328, 701-712 (Pubitemid 41200378)
    • (2005) Comptes Rendus - Biologies , vol.328 , Issue.8 , pp. 701-712
    • Gruebele, M.1
  • 28
    • 34347218159 scopus 로고    scopus 로고
    • Conformational dynamics and ensembles in protein folding
    • DOI 10.1146/annurev.biophys.36.040306.132608
    • Munoz, V. (2007) Conformational dynamics and ensembles in protein folding Annu. Rev. Biophys. Biomol. Struct. 36, 395-412 (Pubitemid 46998125)
    • (2007) Annual Review of Biophysics and Biomolecular Structure , vol.36 , pp. 395-412
    • Munoz, V.1
  • 31
    • 0037111966 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of downhill protein folding investigated with a simple statistical mechanical model
    • Munoz, V. (2002) Thermodynamics and kinetics of downhill protein folding investigated with a simple statistical mechanical model Int. J. Quantum Chem. 90, 1522-1528
    • (2002) Int. J. Quantum Chem. , vol.90 , pp. 1522-1528
    • Munoz, V.1
  • 33
    • 78650415889 scopus 로고    scopus 로고
    • Computational design and experimental testing of the fastest-folding β-sheet protein
    • Piana, S., Sarkar, K., Lindorff-Larsen, K., Guo, M., Gruebele, M., and Shaw, D. E. (2010) Computational design and experimental testing of the fastest-folding β-sheet protein J. Mol. Biol. 405, 43-48
    • (2010) J. Mol. Biol. , vol.405 , pp. 43-48
    • Piana, S.1    Sarkar, K.2    Lindorff-Larsen, K.3    Guo, M.4    Gruebele, M.5    Shaw, D.E.6
  • 36
    • 70450255797 scopus 로고    scopus 로고
    • Constructing the equilibrium ensemble of folding pathways from short off-equilibrium simulations
    • Noe, F., Schutte, C., Vanden-Eijnden, E., Reich, L., and Weikl, T. R. (2009) Constructing the equilibrium ensemble of folding pathways from short off-equilibrium simulations Proc. Natl. Acad. Sci. U.S.A. 106, 19011-19016
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 19011-19016
    • Noe, F.1    Schutte, C.2    Vanden-Eijnden, E.3    Reich, L.4    Weikl, T.R.5
  • 37
  • 38
    • 0037126290 scopus 로고    scopus 로고
    • Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
    • DOI 10.1038/nature01060
    • Schuler, B., Lipman, E. A., and Eaton, W. A. (2002) Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy Nature 419, 743-747 (Pubitemid 35177962)
    • (2002) Nature , vol.419 , Issue.6908 , pp. 743-747
    • Schuler, B.1    Lipman, E.A.2    Eaton, W.A.3
  • 39
    • 33746102627 scopus 로고    scopus 로고
    • Atom-by-atom analysis of global downhill protein folding
    • DOI 10.1038/nature04859, PII NATURE04859
    • Sadqi, M., Fushman, D., and Munoz, V. (2006) Atom-by-atom analysis of global downhill protein folding Nature 442, 317-321 (Pubitemid 44114908)
    • (2006) Nature , vol.442 , Issue.7100 , pp. 317-321
    • Sadqi, M.1    Fushman, D.2    Munoz, V.3
  • 40
    • 38049108092 scopus 로고    scopus 로고
    • Exploring the cooperativity of the fast folding reaction of a small protein using pulsed thiol labeling and mass spectrometry
    • Jha, S. K. and Udgaonkar, J. B. (2007) Exploring the cooperativity of the fast folding reaction of a small protein using pulsed thiol labeling and mass spectrometry J. Biol. Chem. 282, 37479-37491
    • (2007) J. Biol. Chem. , vol.282 , pp. 37479-37491
    • Jha, S.K.1    Udgaonkar, J.B.2
  • 41
    • 77957752175 scopus 로고    scopus 로고
    • Evidence for initial non-specific polypeptide chain collapse during the refolding of the SH3 domain of PI3 kinase
    • Dasgupta, A. and Udgaonkar, J. B. (2010) Evidence for initial non-specific polypeptide chain collapse during the refolding of the SH3 domain of PI3 kinase J. Mol. Biol. 403, 430-445
    • (2010) J. Mol. Biol. , vol.403 , pp. 430-445
    • Dasgupta, A.1    Udgaonkar, J.B.2
  • 42
    • 0036438892 scopus 로고    scopus 로고
    • Differential salt-induced stabilization of structure in the initial folding intermediate ensemble of barstar
    • DOI 10.1016/S0022-2836(02)01068-9
    • Pradeep, L. and Udgaonkar, J. B. (2002) Differential salt-induced stabilization of structure in the initial folding intermediate ensemble of barstar J. Mol. Biol. 324, 331-347 (Pubitemid 35379032)
    • (2002) Journal of Molecular Biology , vol.324 , Issue.2 , pp. 331-347
    • Pradeep, L.1    Udgaonkar, J.B.2
  • 43
    • 0037065672 scopus 로고    scopus 로고
    • Mechanism of formation of a productive molten globule form of barstar
    • DOI 10.1021/bi0120300
    • Rami, B. R. and Udgaonkar, J. B. (2002) Mechanism of formation of a productive molten globule form of barstar Biochemistry 41, 1710-1716 (Pubitemid 34132244)
    • (2002) Biochemistry , vol.41 , Issue.6 , pp. 1710-1716
    • Rami, B.R.1    Udgaonkar, J.B.2
  • 44
    • 33745955427 scopus 로고    scopus 로고
    • Specificity of the Initial Collapse in the Folding of the Cold Shock Protein
    • DOI 10.1016/j.jmb.2006.05.073, PII S0022283606006917
    • Magg, C., Kubelka, J., Holtermann, G., Haas, E., and Schmid, F. X. (2006) Specificity of the initial collapse in the folding of the cold shock protein J. Mol. Biol. 360, 1067-1080 (Pubitemid 44062520)
    • (2006) Journal of Molecular Biology , vol.360 , Issue.5 , pp. 1067-1080
    • Magg, C.1    Kubelka, J.2    Holtermann, G.3    Haas, E.4    Schmid, F.X.5
  • 45
    • 0028915773 scopus 로고
    • Perturbation of a tertiary hydrogen bond in barstar by mutagenesis of the sole His residue to Gln leads to accumulation of at least one equilibrium folding intermediate
    • Nath, U. and Udgaonkar, J. B. (1995) Perturbation of a tertiary hydrogen bond in barstar by mutagenesis of the sole His residue to Gln leads to accumulation of at least one equilibrium folding intermediate Biochemistry 34, 1702-1713
    • (1995) Biochemistry , vol.34 , pp. 1702-1713
    • Nath, U.1    Udgaonkar, J.B.2
  • 46
    • 67650656650 scopus 로고    scopus 로고
    • A single mutation at residue 25 populates the folding intermediate of E. coli RNase H and reveals a highly dynamic partially folded ensemble
    • Connell, K. B., Horner, G. A., and Marqusee, S. (2009) A single mutation at residue 25 populates the folding intermediate of E. coli RNase H and reveals a highly dynamic partially folded ensemble J. Mol. Biol. 391, 461-470
    • (2009) J. Mol. Biol. , vol.391 , pp. 461-470
    • Connell, K.B.1    Horner, G.A.2    Marqusee, S.3
  • 47
    • 0030057477 scopus 로고    scopus 로고
    • Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues
    • DOI 10.1038/nsb0296-193
    • Khorasanizadeh, S., Peters, I. D., and Roder, H. (1996) Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues Nat. Struct. Biol. 3, 193-205 (Pubitemid 26045008)
    • (1996) Nature Structural Biology , vol.3 , Issue.2 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, L.D.2    Roder, H.3
  • 48
    • 0033592403 scopus 로고    scopus 로고
    • A salt-induced kinetic intermediate is on a new parallel pathway of lysozyme folding
    • Bieri, O., Wildegger, G., Bachmann, A., Wagner, C., and Kiefhaber, T. (1999) A salt-induced kinetic intermediate is on a new parallel pathway of lysozyme folding Biochemistry 38, 12460-12470
    • (1999) Biochemistry , vol.38 , pp. 12460-12470
    • Bieri, O.1    Wildegger, G.2    Bachmann, A.3    Wagner, C.4    Kiefhaber, T.5
  • 50
    • 4644261149 scopus 로고    scopus 로고
    • Osmolytes induce structure in an early intermediate on the folding pathway of barstar
    • DOI 10.1074/jbc.M406323200
    • Pradeep, L. and Udgaonkar, J. B. (2004) Osmolytes induce structure in an early intermediate on the folding pathway of barstar J. Biol. Chem. 279, 40303-40313 (Pubitemid 39287615)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.39 , pp. 40303-40313
    • Pradeep, L.1    Udgaonkar, J.B.2
  • 51
    • 33144467755 scopus 로고    scopus 로고
    • Amyloid formation under physiological conditions proceeds via a native-like folding intermediate
    • DOI 10.1038/nsmb1058, PII N1058
    • Jahn, T. R., Parker, M. J., Homans, S. W., and Radford, S. E. (2006) Amyloid formation under physiological conditions proceeds via a native-like folding intermediate Nat. Struct. Mol. Biol. 13, 195-201 (Pubitemid 43348504)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.3 , pp. 195-201
    • Jahn, T.R.1    Parker, M.J.2    Homans, S.W.3    Radford, S.E.4
  • 53
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • DOI 10.1016/S0959-440X(97)80004-8
    • Roder, H. and Colon, W. (1997) Kinetic role of early intermediates in protein folding Curr. Opin. Struct. Biol. 7, 15-28 (Pubitemid 27092376)
    • (1997) Current Opinion in Structural Biology , vol.7 , Issue.1 , pp. 15-28
    • Roder, H.1    Colon, W.2
  • 54
    • 68149147539 scopus 로고    scopus 로고
    • Direct evidence for a dry molten globule intermediate during the unfolding of a small protein
    • Jha, S. K. and Udgaonkar, J. B. (2009) Direct evidence for a dry molten globule intermediate during the unfolding of a small protein Proc. Natl. Acad. Sci. U.S.A. 106, 12289-12294
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 12289-12294
    • Jha, S.K.1    Udgaonkar, J.B.2
  • 55
    • 0021936950 scopus 로고
    • Energetics of protein structure and folding
    • Goldenberg, D. P. and Creighton, T. E. (1985) Energetics of protein structure and folding Biopolymers 24, 167-182
    • (1985) Biopolymers , vol.24 , pp. 167-182
    • Goldenberg, D.P.1    Creighton, T.E.2
  • 56
    • 0030882667 scopus 로고    scopus 로고
    • Thermodynamics of the complex protein unfolding reaction of barstar
    • DOI 10.1021/bi971062d
    • Agashe, V. R., Schmid, F. X., and Udgaonkar, J. B. (1997) Thermodynamics of the complex protein unfolding reaction of barstar Biochemistry 36, 12288-12295 (Pubitemid 27440968)
    • (1997) Biochemistry , vol.36 , Issue.40 , pp. 12288-12295
    • Agashe, V.R.1    Schmid, F.X.2    Udgaonkar, J.B.3
  • 57
    • 61649112900 scopus 로고    scopus 로고
    • Revealing a concealed intermediate that forms after the rate-limiting step of refolding of the SH3 domain of PI3 kinase
    • Wani, A. H. and Udgaonkar, J. B. (2009) Revealing a concealed intermediate that forms after the rate-limiting step of refolding of the SH3 domain of PI3 kinase J. Mol. Biol. 387, 348-362
    • (2009) J. Mol. Biol. , vol.387 , pp. 348-362
    • Wani, A.H.1    Udgaonkar, J.B.2
  • 58
    • 33748774168 scopus 로고    scopus 로고
    • HX-ESI-MS and optical studies of the unfolding of thioredoxin indicate stabilization of a partially unfolded, aggregation-competent intermediate at low pH
    • DOI 10.1021/bi060647h
    • Wani, A. H. and Udgaonkar, J. B. (2006) HX-ESI-MS and optical studies of the unfolding of thioredoxin indicate stabilization of a partially unfolded, aggregation-competent intermediate at low pH Biochemistry 45, 11226-11238 (Pubitemid 44413669)
    • (2006) Biochemistry , vol.45 , Issue.37 , pp. 11226-11238
    • Wani, A.H.1    Udgaonkar, J.B.2
  • 59
    • 77957970492 scopus 로고    scopus 로고
    • Dry molten globule intermediates and the mechanism of protein unfolding
    • Baldwin, R. L., Frieden, C., and Rose, G. D. (2010) Dry molten globule intermediates and the mechanism of protein unfolding Proteins 78, 2725-2737
    • (2010) Proteins , vol.78 , pp. 2725-2737
    • Baldwin, R.L.1    Frieden, C.2    Rose, G.D.3
  • 60
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai, Y., Sosnick, T. R., Mayne, L., and Englander, S. W. (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
  • 61
    • 0037176861 scopus 로고    scopus 로고
    • Characterization of the unfolding of ribonuclease A by a pulsed hydrogen exchange study: Evidence for competing pathways for unfolding
    • DOI 10.1021/bi011480p
    • Juneja, J. and Udgaonkar, J. B. (2002) Characterization of the unfolding of ribonuclease A by a pulsed hydrogen exchange study: Evidence for competing pathways for unfolding Biochemistry 41, 2641-2654 (Pubitemid 34168933)
    • (2002) Biochemistry , vol.41 , Issue.8 , pp. 2641-2654
    • Juneja, J.1    Udgaonkar, J.B.2
  • 62
    • 0032570543 scopus 로고    scopus 로고
    • Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy
    • DOI 10.1006/jmbi.1997.1553
    • Guijarro, J. I., Morton, C. J., Plaxco, K. W., Campbell, I. D., and Dobson, C. M. (1998) Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy J. Mol. Biol. 276, 657-667 (Pubitemid 28116136)
    • (1998) Journal of Molecular Biology , vol.276 , Issue.3 , pp. 657-667
    • Guijarro, J.I.1    Morton, C.J.2    Plaxco, K.W.3    Campbell, I.D.4    Dobson, C.M.5
  • 63
    • 30344457011 scopus 로고    scopus 로고
    • Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation
    • DOI 10.1016/j.jmb.2005.11.034, PII S0022283605014221
    • Bader, R., Bamford, R., Zurdo, J., Luisi, B. F., and Dobson, C. M. (2006) Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation J. Mol. Biol. 356, 189-208 (Pubitemid 43069737)
    • (2006) Journal of Molecular Biology , vol.356 , Issue.1 , pp. 189-208
    • Bader, R.1    Bamford, R.2    Zurdo, J.3    Luisi, B.F.4    Dobson, C.M.5
  • 64
    • 0030467027 scopus 로고    scopus 로고
    • 2
    • DOI 10.1021/bi961976k
    • Sauder, J. M., MacKenzie, N. E., and Roder, H. (1996) Kinetic mechanism of folding and unfolding of Rhodobacter capsulatus cytochrome c2 Biochemistry 35, 16852-16862 (Pubitemid 27020531)
    • (1996) Biochemistry , vol.35 , Issue.51 , pp. 16852-16862
    • Sauder, J.M.1    MacKenzie, N.E.2    Roder, H.3
  • 66
    • 0013800421 scopus 로고
    • The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites
    • Stryer, L. (1965) The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites J. Mol. Biol. 13, 482-495
    • (1965) J. Mol. Biol. , vol.13 , pp. 482-495
    • Stryer, L.1
  • 67
    • 0028802181 scopus 로고
    • Initial hydrophobic collapse in the folding of barstar
    • Agashe, V. R., Shastry, M. C., and Udgaonkar, J. B. (1995) Initial hydrophobic collapse in the folding of barstar Nature 377, 754-757
    • (1995) Nature , vol.377 , pp. 754-757
    • Agashe, V.R.1    Shastry, M.C.2    Udgaonkar, J.B.3
  • 68
    • 0034665642 scopus 로고    scopus 로고
    • The slow folding reaction of barstar: The core tryptophan region attains tight packing before substantial secondary and tertiary structure formation and final compaction of the polypeptide chain
    • Sridevi, K., Juneja, J., Bhuyan, A. K., Krishnamoorthy, G., and Udgaonkar, J. B. (2000) The slow folding reaction of barstar: The core tryptophan region attains tight packing before substantial secondary and tertiary structure formation and final compaction of the polypeptide chain J. Mol. Biol. 302, 479-495
    • (2000) J. Mol. Biol. , vol.302 , pp. 479-495
    • Sridevi, K.1    Juneja, J.2    Bhuyan, A.K.3    Krishnamoorthy, G.4    Udgaonkar, J.B.5
  • 69
    • 0013807126 scopus 로고
    • On the conformational stability of globular proteins. The effects of various electrolytes and nonelectrolytes on the thermal ribonuclease transition
    • Von Hippel, P. H. and Wong, K. Y. (1965) On the conformational stability of globular proteins. The effects of various electrolytes and nonelectrolytes on the thermal ribonuclease transition J. Biol. Chem. 240, 3909-3923
    • (1965) J. Biol. Chem. , vol.240 , pp. 3909-3923
    • Von Hippel, P.H.1    Wong, K.Y.2
  • 70
    • 0020477047 scopus 로고
    • Preferential interactions of proteins with salts in concentrated solutions
    • Arakawa, T. and Timasheff, S. N. (1982) Preferential interactions of proteins with salts in concentrated solutions Biochemistry 21, 6545-6552
    • (1982) Biochemistry , vol.21 , pp. 6545-6552
    • Arakawa, T.1    Timasheff, S.N.2
  • 71
    • 33646186493 scopus 로고    scopus 로고
    • Salting the charged surface: PH and salt dependence of protein G B1 stability
    • Lindman, S., Xue, W. F., Szczepankiewicz, O., Bauer, M. C., Nilsson, H., and Linse, S. (2006) Salting the charged surface: pH and salt dependence of protein G B1 stability Biophys. J. 90, 2911-2921
    • (2006) Biophys. J. , vol.90 , pp. 2911-2921
    • Lindman, S.1    Xue, W.F.2    Szczepankiewicz, O.3    Bauer, M.C.4    Nilsson, H.5    Linse, S.6
  • 72
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • Baldwin, R. L. (1996) How Hofmeister ion interactions affect protein stability Biophys. J. 71, 2056-2063 (Pubitemid 26325984)
    • (1996) Biophysical Journal , vol.71 , Issue.4 , pp. 2056-2063
    • Baldwin, R.L.1
  • 73
    • 0036081128 scopus 로고    scopus 로고
    • Sulfate anion stabilization of native ribonuclease A both by anion binding and by the Hofmeister effect
    • DOI 10.1110/ps.0205902
    • Ramos, C. H. and Baldwin, R. L. (2002) Sulfate anion stabilization of native ribonuclease A both by anion binding and by the Hofmeister effect Protein Sci. 11, 1771-1778 (Pubitemid 34663556)
    • (2002) Protein Science , vol.11 , Issue.7 , pp. 1771-1778
    • Ramos, C.H.I.1    Baldwin, R.L.2
  • 74
    • 0022147096 scopus 로고
    • The Hofmeister effect and the behaviour of water at interfaces
    • Collins, K. D. and Washabaugh, M. W. (1985) The Hofmeister effect and the behaviour of water at interfaces Q. Rev. Biophys. 18, 323-422
    • (1985) Q. Rev. Biophys. , vol.18 , pp. 323-422
    • Collins, K.D.1    Washabaugh, M.W.2
  • 75
    • 0025030410 scopus 로고
    • A simple model for solvation in mixed solvents. Applications to the stabilization and destabilization of macromolecular structures
    • DOI 10.1016/0301-4622(90)88013-I
    • Schellman, J. A. (1990) A simple model for solvation in mixed solvents. Applications to the stabilization and destabilization of macromolecular structures Biophys. Chem. 37, 121-140 (Pubitemid 20287782)
    • (1990) Biophysical Chemistry , vol.37 , Issue.1-3 , pp. 121-140
    • Schellman, J.A.1
  • 76
    • 0031776135 scopus 로고    scopus 로고
    • Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: A practical guide to recognizing and interpreting polyelectrolyte effects, Hofmeister effects, and osmotic effects of salts
    • Record, M. T., Jr., Zhang, W., and Anderson, C. F. (1998) Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: A practical guide to recognizing and interpreting polyelectrolyte effects, Hofmeister effects, and osmotic effects of salts Adv. Protein Chem. 51, 281-353
    • (1998) Adv. Protein Chem. , vol.51 , pp. 281-353
    • Record Jr., M.T.1    Zhang, W.2    Anderson, C.F.3
  • 77
    • 13444250971 scopus 로고    scopus 로고
    • Apparent Debye-Huckel electrostatic effects in the folding of a simple, single domain protein
    • DOI 10.1021/bi048444l
    • de Los Rios, M. A. and Plaxco, K. W. (2005) Apparent Debye-Huckel electrostatic effects in the folding of a simple, single domain protein Biochemistry 44, 1243-1250 (Pubitemid 40209004)
    • (2005) Biochemistry , vol.44 , Issue.4 , pp. 1243-1250
    • De Los Rios, M.A.1    Plaxco, K.W.2
  • 79
    • 0037079586 scopus 로고    scopus 로고
    • Is there a unique melting temperature for two-state proteins?
    • DOI 10.1002/jcc.10005
    • Klimov, D. K. and Thirumalai, D. (2002) Is there a unique melting temperature for two-state proteins? J. Comput. Chem. 23, 161-165 (Pubitemid 34063140)
    • (2002) Journal of Computational Chemistry , vol.23 , Issue.1 , pp. 161-165
    • Klimov, D.K.1    Thirumalai, D.2
  • 80
    • 0029155772 scopus 로고
    • Impact of local and non-local interactions on thermodynamics and kinetics of protein folding
    • Abkevich, V. I., Gutin, A. M., and Shakhnovich, E. I. (1995) Impact of local and non-local interactions on thermodynamics and kinetics of protein folding J. Mol. Biol. 252, 460-471
    • (1995) J. Mol. Biol. , vol.252 , pp. 460-471
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 81
    • 84984082911 scopus 로고
    • Statistical Mechanics of Noncovalent Bonds in Polyamino Acids. IX. 2-State Theory of Protein Denaturation
    • Poland, D. C. and Scheraga, H. A. (1965) Statistical Mechanics of Noncovalent Bonds in Polyamino Acids. IX. 2-State Theory of Protein Denaturation Biopolymers 3, 401-419
    • (1965) Biopolymers , vol.3 , pp. 401-419
    • Poland, D.C.1    Scheraga, H.A.2
  • 82
    • 78049378463 scopus 로고    scopus 로고
    • The effect of electrostatics on the marginal cooperativity of an ultrafast folding protein
    • Desai, T. M., Cerminara, M., Sadqi, M., and Munoz, V. (2010) The effect of electrostatics on the marginal cooperativity of an ultrafast folding protein J. Biol. Chem. 285, 34549-34556
    • (2010) J. Biol. Chem. , vol.285 , pp. 34549-34556
    • Desai, T.M.1    Cerminara, M.2    Sadqi, M.3    Munoz, V.4
  • 83
    • 0030694241 scopus 로고    scopus 로고
    • Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations
    • DOI 10.1038/nsb1197-925
    • Luo, Y., Kay, M. S., and Baldwin, R. L. (1997) Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations Nat. Struct. Biol. 4, 925-930 (Pubitemid 27479444)
    • (1997) Nature Structural Biology , vol.4 , Issue.11 , pp. 925-930
    • Luo, Y.1    Kay, M.S.2    Baldwin, R.L.3
  • 84
    • 0033550298 scopus 로고    scopus 로고
    • The cooperativity of burst phase reactions explored
    • Parker, M. J. and Marqusee, S. (1999) The cooperativity of burst phase reactions explored J. Mol. Biol. 293, 1195-1210
    • (1999) J. Mol. Biol. , vol.293 , pp. 1195-1210
    • Parker, M.J.1    Marqusee, S.2
  • 85
    • 26244466045 scopus 로고    scopus 로고
    • Dependence of the size of the initially collapsed form during the refolding of barstar on denaturant concentration: Evidence for a continuous transition
    • DOI 10.1016/j.jmb.2005.08.056, PII S0022283605010107
    • Sinha, K. K. and Udgaonkar, J. B. (2005) Dependence of the size of the initially collapsed form during the refolding of barstar on denaturant concentration: Evidence for a continuous transition J. Mol. Biol. 353, 704-718 (Pubitemid 41414742)
    • (2005) Journal of Molecular Biology , vol.353 , Issue.3 , pp. 704-718
    • Sinha, K.K.1    Udgaonkar, J.B.2
  • 86
    • 34249748424 scopus 로고    scopus 로고
    • Dissecting the Non-specific and Specific Components of the Initial Folding Reaction of Barstar by Multi-site FRET Measurements
    • DOI 10.1016/j.jmb.2007.04.061, PII S002228360700561X
    • Sinha, K. K. and Udgaonkar, J. B. (2007) Dissecting the non-specific and specific components of the initial folding reaction of barstar by multi-site FRET measurements J. Mol. Biol. 370, 385-405 (Pubitemid 46830925)
    • (2007) Journal of Molecular Biology , vol.370 , Issue.2 , pp. 385-405
    • Sinha, K.K.1    Udgaonkar, J.B.2
  • 88
    • 34247880253 scopus 로고    scopus 로고
    • Protein folding kinetics: Barrier effects in chemical and thermal denaturation experiments
    • DOI 10.1021/ja0689740
    • Naganathan, A. N., Doshi, U., and Munoz, V. (2007) Protein folding kinetics: Barrier effects in chemical and thermal denaturation experiments J. Am. Chem. Soc. 129, 5673-5682 (Pubitemid 46697657)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.17 , pp. 5673-5682
    • Naganathan, A.N.1    Doshi, U.2    Munoz, V.3
  • 92
    • 0029115374 scopus 로고
    • Kinetics of interaction of partially folded proteins with a hydrophobic dye: Evidence that molten globule character is maximal in early folding intermediates
    • Engelhard, M. and Evans, P. A. (1995) Kinetics of interaction of partially folded proteins with a hydrophobic dye: Evidence that molten globule character is maximal in early folding intermediates Protein Sci. 4, 1553-1562
    • (1995) Protein Sci. , vol.4 , pp. 1553-1562
    • Engelhard, M.1    Evans, P.A.2
  • 94
    • 0024745242 scopus 로고
    • Theory of cooperative transitions in protein molecules. II. Phase diagram for a protein molecule in solution
    • Finkelstein, A. V. and Shakhnovich, E. I. (1989) Theory of cooperative transitions in protein molecules. II. Phase diagram for a protein molecule in solution Biopolymers 28, 1681-1694
    • (1989) Biopolymers , vol.28 , pp. 1681-1694
    • Finkelstein, A.V.1    Shakhnovich, E.I.2
  • 95
    • 0029913321 scopus 로고    scopus 로고
    • A scanning calorimetric study of unfolding equilibria in homodimeric chicken gizzard tropomyosins
    • O'Brien, R., Sturtevant, J. M., Wrabl, J., Holtzer, M. E., and Holtzer, A. (1996) A scanning calorimetric study of unfolding equilibria in homodimeric chicken gizzard tropomyosins Biophys. J. 70, 2403-2407 (Pubitemid 26133735)
    • (1996) Biophysical Journal , vol.70 , Issue.5 , pp. 2403-2407
    • O'Brien, R.1    Sturtevant, J.M.2    Wrabl, J.3    Holtzer, M.E.4    Holtzer, A.5
  • 96
    • 0029975396 scopus 로고    scopus 로고
    • Motional dynamics of a buried tryptophan reveals the presence of partially structured forms during denaturation of barstar
    • DOI 10.1021/bi9603478
    • Swaminathan, R., Nath, U., Udgaonkar, J. B., Periasamy, N., and Krishnamoorthy, G. (1996) Motional dynamics of a buried tryptophan reveals the presence of partially structured forms during denaturation of barstar Biochemistry 35, 9150-9157 (Pubitemid 26249863)
    • (1996) Biochemistry , vol.35 , Issue.28 , pp. 9150-9157
    • Swaminathan, R.1    Nath, U.2    Udgaonkar, J.B.3    Periasamy, N.4    Krishnamoorthy, G.5
  • 97
    • 0038047141 scopus 로고    scopus 로고
    • Dynamics of the core tryptophan during the formation of a productive molten globule intermediate of barstar
    • DOI 10.1021/bi030006b
    • Rami, B. R., Krishnamoorthy, G., and Udgaonkar, J. B. (2003) Dynamics of the core tryptophan during the formation of a productive molten globule intermediate of barstar Biochemistry 42, 7986-8000 (Pubitemid 36807716)
    • (2003) Biochemistry , vol.42 , Issue.26 , pp. 7986-8000
    • Rami, B.R.1    Krishnamoorthy, G.2    Udgaonkar, J.B.3
  • 98
    • 23744503388 scopus 로고    scopus 로고
    • UV-resonance Raman thermal unfolding study of Trp-cage shows that it is not a simple two-state miniprotein
    • DOI 10.1021/ja050664e
    • Ahmed, Z., Beta, I. A., Mikhonin, A. V., and Asher, S. A. (2005) UV-resonance Raman thermal unfolding study of Trp-cage shows that it is not a simple two-state miniprotein J. Am. Chem. Soc. 127, 10943-10950 (Pubitemid 41129869)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.31 , pp. 10943-10950
    • Ahmed, Z.1    Beta, I.A.2    Mikhonin, A.V.3    Asher, S.A.4
  • 99
    • 0030347877 scopus 로고    scopus 로고
    • On-pathway versus off-pathway folding intermediates
    • Baldwin, R. L. (1996) On-pathway versus off-pathway folding intermediates Folding Des. 1, R1-R8
    • (1996) Folding Des. , vol.1
    • Baldwin, R.L.1
  • 100
    • 0030796986 scopus 로고    scopus 로고
    • Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate
    • DOI 10.1006/jmbi.1997.1030
    • Wildegger, G. and Kiefhaber, T. (1997) Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate J. Mol. Biol. 270, 294-304 (Pubitemid 27296689)
    • (1997) Journal of Molecular Biology , vol.270 , Issue.2 , pp. 294-304
    • Wildegger, G.1    Kiefhaber, T.2
  • 101
    • 0035812628 scopus 로고    scopus 로고
    • Folding of horse cytochrome c in the reduced state
    • DOI 10.1006/jmbi.2001.4993
    • Bhuyan, A. K. and Udgaonkar, J. B. (2001) Folding of horse cytochrome c in the reduced state J. Mol. Biol. 312, 1135-1160 (Pubitemid 32980331)
    • (2001) Journal of Molecular Biology , vol.312 , Issue.5 , pp. 1135-1160
    • Bhuyan, A.K.1    Udgaonkar, J.B.2


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