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Volumn 17, Issue 1, 2008, Pages 43-53

Folding thermodynamics and kinetics of the leucine-rich repeat domain of the virulence factor Internalin B

Author keywords

Kinetics; Leucine rich repeat; Protein folding; Repeat protein

Indexed keywords

INTERNALIN B; LEUCINE; UNCLASSIFIED DRUG; UREA; VIRULENCE FACTOR;

EID: 37549036251     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.073166608     Document Type: Article
Times cited : (23)

References (40)
  • 1
    • 0030347877 scopus 로고    scopus 로고
    • On-pathway versus off-pathway folding intermediates
    • Baldwin, R.L. 1996. On-pathway versus off-pathway folding intermediates. Fold. Des. 1: R1-R8.
    • (1996) Fold. Des , vol.1
    • Baldwin, R.L.1
  • 2
    • 1542666874 scopus 로고    scopus 로고
    • GW domains of the Listeria monocytogenes invasion protein InlB are required for potentiation of Met activation
    • Banerjee, M., Copp, J., Vuga, D., Marino, M., Chapman, T., van der Geer, P., and Ghosh, P. 2004. GW domains of the Listeria monocytogenes invasion protein InlB are required for potentiation of Met activation. Mol. Microbiol. 52: 257-271.
    • (2004) Mol. Microbiol , vol.52 , pp. 257-271
    • Banerjee, M.1    Copp, J.2    Vuga, D.3    Marino, M.4    Chapman, T.5    van der Geer, P.6    Ghosh, P.7
  • 3
    • 0024291318 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 2. Incorporation of ΔG degrees N-U values in a thermodynamic cycle
    • Bolen, D.W. and Santoro, M.M. 1988. Unfolding free energy changes determined by the linear extrapolation method. 2. Incorporation of ΔG degrees N-U values in a thermodynamic cycle. Biochemistry 27: 8069-8074.
    • (1988) Biochemistry , vol.27 , pp. 8069-8074
    • Bolen, D.W.1    Santoro, M.M.2
  • 4
    • 23944525891 scopus 로고    scopus 로고
    • Effect of multiple prolyl isomerization reactions on the stability and folding kinetics of the Notch ankyrin domain: Experiment and theory
    • Bradley, C.M. and Barrick, D. 2005. Effect of multiple prolyl isomerization reactions on the stability and folding kinetics of the Notch ankyrin domain: Experiment and theory. J. Mol. Biol. 352: 253-265.
    • (2005) J. Mol. Biol , vol.352 , pp. 253-265
    • Bradley, C.M.1    Barrick, D.2
  • 5
    • 33746841062 scopus 로고    scopus 로고
    • The Notch ankyrin domain folds via a discrete, centralized pathway
    • Bradley, C.M. and Barrick, D. 2006. The Notch ankyrin domain folds via a discrete, centralized pathway. Structure 14: 1303-1312.
    • (2006) Structure , vol.14 , pp. 1303-1312
    • Bradley, C.M.1    Barrick, D.2
  • 6
    • 0016711868 scopus 로고
    • Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
    • Brandts, J.F., Halvorson, H.R., and Brennan, M. 1975. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry 14: 4953-4963.
    • (1975) Biochemistry , vol.14 , pp. 4953-4963
    • Brandts, J.F.1    Halvorson, H.R.2    Brennan, M.3
  • 7
    • 0032817183 scopus 로고    scopus 로고
    • A capping domain for LRR protein interaction modules
    • Ceulemans, H., De Maeyer, M., Stalmans, W., and Bollen, M. 1999. A capping domain for LRR protein interaction modules. FEBS Lett. 456: 349-351.
    • (1999) FEBS Lett , vol.456 , pp. 349-351
    • Ceulemans, H.1    De Maeyer, M.2    Stalmans, W.3    Bollen, M.4
  • 8
    • 1442323733 scopus 로고    scopus 로고
    • Folding and stability of the leucine-rich repeat domain of internalin B from Listeria monocytogenes
    • Freiberg, A., Machner, M.P., Pfeil, W., Schubert, W.D., Heinz, D.W., and Seckler, R. 2004. Folding and stability of the leucine-rich repeat domain of internalin B from Listeria monocytogenes. J. Mol. Biol. 337: 453-461.
    • (2004) J. Mol. Biol , vol.337 , pp. 453-461
    • Freiberg, A.1    Machner, M.P.2    Pfeil, W.3    Schubert, W.D.4    Heinz, D.W.5    Seckler, R.6
  • 9
    • 34250802262 scopus 로고    scopus 로고
    • The crystal structure of the tumor suppressor protein pp32 (Anp32a): Structural insights into Anp32 family of proteins
    • Huyton, T. and Wolberger, C. 2007. The crystal structure of the tumor suppressor protein pp32 (Anp32a): Structural insights into Anp32 family of proteins. Protein Sci. 16: 1308-1315.
    • (2007) Protein Sci , vol.16 , pp. 1308-1315
    • Huyton, T.1    Wolberger, C.2
  • 10
    • 33645525759 scopus 로고    scopus 로고
    • Pertactin β-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins
    • Junker, M., Schuster, C.C., McDonnell, A.V., Sorg, K.A., Finn, M.C., Berger, B., and Clark, P.L. 2006. Pertactin β-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins. Proc. Natl. Acad. Sci. 103: 4918-4923.
    • (2006) Proc. Natl. Acad. Sci , vol.103 , pp. 4918-4923
    • Junker, M.1    Schuster, C.C.2    McDonnell, A.V.3    Sorg, K.A.4    Finn, M.C.5    Berger, B.6    Clark, P.L.7
  • 12
    • 0034808018 scopus 로고    scopus 로고
    • A partially folded intermediate conformation is induced in pectate lyase C by the addition of 8-anilino-1-naphthalenesulfonate (ANS)
    • Kamen, D.E. and Woody, R.W. 2001. A partially folded intermediate conformation is induced in pectate lyase C by the addition of 8-anilino-1-naphthalenesulfonate (ANS). Protein Sci. 10: 2123-2130.
    • (2001) Protein Sci , vol.10 , pp. 2123-2130
    • Kamen, D.E.1    Woody, R.W.2
  • 13
    • 0034719144 scopus 로고    scopus 로고
    • The stability, structural organization, and denaturation of pectate lyase C, a parallel β-helix protein
    • Kamen, D.E., Griko, Y., and Woody, R.W. 2000. The stability, structural organization, and denaturation of pectate lyase C, a parallel β-helix protein. Biochemistry 39: 15932-15943.
    • (2000) Biochemistry , vol.39 , pp. 15932-15943
    • Kamen, D.E.1    Griko, Y.2    Woody, R.W.3
  • 14
    • 0026516420 scopus 로고
    • Kinetic coupling between protein folding and prolyl isomerization. I. Theoretical models
    • Kiefhaber, T., Kohler, H.H., and Schmid, F.X. 1992. Kinetic coupling between protein folding and prolyl isomerization. I. Theoretical models. J. Mol. Biol. 224: 217-229.
    • (1992) J. Mol. Biol , vol.224 , pp. 217-229
    • Kiefhaber, T.1    Kohler, H.H.2    Schmid, F.X.3
  • 16
    • 36749050344 scopus 로고    scopus 로고
    • Repeat protein folding: New insights into origins of cooperativity, stability, and topology
    • in press, doi: 10.1016/j.abb.2007.08.03.4
    • Kloss, E., Courtemanche, N., and Barrick, D. 2007. Repeat protein folding: New insights into origins of cooperativity, stability, and topology. Arch. Biochem. Biophys. (in press). doi: 10.1016/j.abb.2007.08.03.4.
    • (2007) Arch. Biochem. Biophys
    • Kloss, E.1    Courtemanche, N.2    Barrick, D.3
  • 17
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima, K. 1989. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins 6: 87-103.
    • (1989) Proteins , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 18
    • 0026005997 scopus 로고
    • Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy
    • Kuwajima, K., Garvey, E.P., Finn, B.E., Matthews, C.R., and Sugai, S. 1991. Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy. Biochemistry 30: 7693-7703.
    • (1991) Biochemistry , vol.30 , pp. 7693-7703
    • Kuwajima, K.1    Garvey, E.P.2    Finn, B.E.3    Matthews, C.R.4    Sugai, S.5
  • 19
    • 0025216877 scopus 로고
    • Cloning, expression, and purification of human cyclophilin in Escherichia coli and assessment of the catalytic role of cysteines by site-directed mutagenesis
    • Liu, J., Albers, M.W., Chen, C.M., Schreiber, S.L., and Walsh, C.T. 1990. Cloning, expression, and purification of human cyclophilin in Escherichia coli and assessment of the catalytic role of cysteines by site-directed mutagenesis. Proc. Natl. Acad. Sci. 87: 2304-2308.
    • (1990) Proc. Natl. Acad. Sci , vol.87 , pp. 2304-2308
    • Liu, J.1    Albers, M.W.2    Chen, C.M.3    Schreiber, S.L.4    Walsh, C.T.5
  • 20
    • 33845874375 scopus 로고    scopus 로고
    • Biophysical characterisation of the small ankyrin repeat protein myotrophin
    • Lowe, A.R. and Itzhaki, L.S. 2007a. Biophysical characterisation of the small ankyrin repeat protein myotrophin. J. Mol. Biol. 365: 1245-1255.
    • (2007) J. Mol. Biol , vol.365 , pp. 1245-1255
    • Lowe, A.R.1    Itzhaki, L.S.2
  • 21
    • 33847328451 scopus 로고    scopus 로고
    • Rational redesign of the folding pathway of a modular protein
    • Lowe, A.R. and Itzhaki, L.S. 2007b. Rational redesign of the folding pathway of a modular protein. Proc. Natl. Acad. Sci. 104: 2679-2684.
    • (2007) Proc. Natl. Acad. Sci , vol.104 , pp. 2679-2684
    • Lowe, A.R.1    Itzhaki, L.S.2
  • 22
    • 0027190920 scopus 로고
    • Structure and stability of an early folding intermediate of Escherichia coli trp aporepressor measured by far-UV stopped-flow circular dichroism and 8-anilino-1-naphthalene sulfonate binding
    • Mann, C.J. and Matthews, C.R. 1993. Structure and stability of an early folding intermediate of Escherichia coli trp aporepressor measured by far-UV stopped-flow circular dichroism and 8-anilino-1-naphthalene sulfonate binding. Biochemistry 32: 5282-5290.
    • (1993) Biochemistry , vol.32 , pp. 5282-5290
    • Mann, C.J.1    Matthews, C.R.2
  • 23
    • 0033256246 scopus 로고    scopus 로고
    • Structure of the lnlB leucine-rich repeats, a domain that triggers host cell invasion by the bacterial pathogen L. monocytogenes
    • Marino, M., Braun, L., Cossart, P., and Ghosh, P. 1999. Structure of the lnlB leucine-rich repeats, a domain that triggers host cell invasion by the bacterial pathogen L. monocytogenes. Mol. Cell 4: 1063-1072.
    • (1999) Mol. Cell , vol.4 , pp. 1063-1072
    • Marino, M.1    Braun, L.2    Cossart, P.3    Ghosh, P.4
  • 24
    • 4644306518 scopus 로고    scopus 로고
    • An experimentally determined protein folding energy landscape
    • Mello, C.C. and Barrick, D. 2004. An experimentally determined protein folding energy landscape. Proc. Natl. Acad. Sci. 101: 14102-14107.
    • (2004) Proc. Natl. Acad. Sci , vol.101 , pp. 14102-14107
    • Mello, C.C.1    Barrick, D.2
  • 25
    • 23944479773 scopus 로고    scopus 로고
    • Experimental characterization of the folding kinetics of the Notch ankyrin domain
    • Mello, C.C., Bradley, C.M., Tripp, K.W., and Barrick, D. 2005. Experimental characterization of the folding kinetics of the Notch ankyrin domain. J. Mol. Biol. 352: 266-281.
    • (2005) J. Mol. Biol , vol.352 , pp. 266-281
    • Mello, C.C.1    Bradley, C.M.2    Tripp, K.W.3    Barrick, D.4
  • 26
    • 0036298327 scopus 로고    scopus 로고
    • Equilibrium folding and stability of myotrophin: A model ankyrin repeat protein
    • Mosavi, L.K., Williams, S., and Peng, Z.Y. 2002. Equilibrium folding and stability of myotrophin: A model ankyrin repeat protein. J. Mol. Biol. 320: 165-170.
    • (2002) J. Mol. Biol , vol.320 , pp. 165-170
    • Mosavi, L.K.1    Williams, S.2    Peng, Z.Y.3
  • 27
    • 0035997388 scopus 로고    scopus 로고
    • Mechanism of fast protein folding
    • Myers, J.K. and Oas, T.G. 2002. Mechanism of fast protein folding. Annu. Rev. Biochem. 71: 783-815.
    • (2002) Annu. Rev. Biochem , vol.71 , pp. 783-815
    • Myers, J.K.1    Oas, T.G.2
  • 28
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers, J.K., Pace, C.N., and Scholtz, J.M. 1995. Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4: 2138-2148.
    • (1995) Protein Sci , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 29
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C.N. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131: 266-280.
    • (1986) Methods Enzymol , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 30
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • 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.
    • (1998) J. Mol. Biol , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 31
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro, M.M. and Bolen, D.W. 1988. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry 27: 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 32
    • 0001340839 scopus 로고
    • Kinetics of unfolding and refolding of single-domain proteins
    • ed. T.E. Creighton, pp, W.H. Freeman, New York
    • Schmid, F.X. 1992. Kinetics of unfolding and refolding of single-domain proteins. In Protein folding. (ed. T.E. Creighton), pp. 197-241. W.H. Freeman, New York.
    • (1992) Protein folding , pp. 197-241
    • Schmid, F.X.1
  • 33
    • 0031919973 scopus 로고    scopus 로고
    • Evidence for barrier-limited protein folding kinetics on the microsecond timescale
    • Shastry, M.C. and Roder, H. 1998. Evidence for barrier-limited protein folding kinetics on the microsecond timescale. Nat. Struct. Biol. 5: 385-392.
    • (1998) Nat. Struct. Biol , vol.5 , pp. 385-392
    • Shastry, M.C.1    Roder, H.2
  • 34
    • 1642368109 scopus 로고    scopus 로고
    • Analysis of heterologous interacting systems by sedimentation velocity: Curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants
    • Stafford, W.F. and Sherwood, P.J. 2004. Analysis of heterologous interacting systems by sedimentation velocity: Curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants. Biophys. Chem. 108: 231-243.
    • (2004) Biophys. Chem , vol.108 , pp. 231-243
    • Stafford, W.F.1    Sherwood, P.J.2
  • 35
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford, C. 1968. Protein denaturation. Adv. Protein Chem. 23: 121-282.
    • (1968) Adv. Protein Chem , vol.23 , pp. 121-282
    • Tanford, C.1
  • 36
    • 0014718113 scopus 로고
    • Protein denaturation. C. Theoretical models for the mechanism of denaturation
    • Tanford, C. 1970. Protein denaturation. C. Theoretical models for the mechanism of denaturation. Adv. Protein Chem. 24: 1-95.
    • (1970) Adv. Protein Chem , vol.24 , pp. 1-95
    • Tanford, C.1
  • 40
    • 0035807936 scopus 로고    scopus 로고
    • Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor. 2. Solution stability and cooperativity of unfolding
    • Zweifel, M.E. and Barrick, D. 2001. Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor. 2. Solution stability and cooperativity of unfolding. Biochemistry 40: 14357-14367.
    • (2001) Biochemistry , vol.40 , pp. 14357-14367
    • Zweifel, M.E.1    Barrick, D.2


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