Structural Zn(II) Implies a Switch from Fully Cooperative to Partly Downhill Folding in Highly Homologous Proteins (408 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2013 Apr 2; 135(13): 5220-5228.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 11.444, 5-year impact factor: 11.015
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84875797582&partnerID=40&md5=265e8956facb9aafd785c05d92042914
Keywords: Biological Process, Homologous Proteins, Intermediate State, Protein Folding Reaction, Protein Misfolding, Structural Feature, Thermal Unfolding, Zinc Finger Domains, Metal Ions, Random Processes, Thermodynamics, Zinc Compounds, Zinc Finger Protein, Article, Circular Dichroism, Differential Scanning Calorimetry, Molecular Mechanics, Nonhuman, Nuclear Magnetic Resonance, Prokaryotic Cell, Protein Structure, Magnetic Resonance Spectroscopy, Models,
Affiliations:
*** IBB - CNR ***
Department of Environmental, Biological and Pharmaceutical Science and Technology, Second University of Naples, Via Vivaldi 43, 81100 Caserta, Italy
Institute of Biostructures and Bioimaging-CNR (Naples), Via Mezzocannone 16, 80134 Naples, Italy
References:
Tanford, C., (1968) Adv. Protein Chem., 23, p. 12
Bryngelson, J.D., Onuchic, J.N., Socci, N.D., Wolynes, P.G., (1995) Proteins, 21, p. 167
Halskau, O., Perez-Jimenez, R., Ibarra-Molero, B., Underhaug, J., Muñoz, V., Martinez, A., Sanchez-Ruiz, J.M., (2008) Proc. Natl. Acad. Sci. U.S.A., 105, p. 8625
Sadqi, M., Fushman, D., Muñoz, V., (2006) Nature, 442, p. 317
Brockwell, D.J., Radford, S.E., (2007) Curr. Opin. Struct. Biol., 17, p. 30
Korzhnev, D.M., Salvatella, X., Vendruscolo, M., Di Nardo, A.A., Davidson, A.R., Dobson, C.M., Kay, L.E., (2004) Nature, 430, p. 586
Chen, Y., Ding, F., Nie, H., Serohijos, A.W., Sharma, S., Wilcox, K.C., Yin, S., Dokholyan, N.V., (2008) Arch. Biochem. Biophys., 469, p. 4
Coyne, H.J., Ciofi-Baffoni, S., Banci, L., Bertini, I., Zhang, L., George, G.N., Winge, D.R., (2007) J. Biol. Chem., 282, p. 8926
Ikeguchi, M., Kuwajima, K., Sugai, S., (1986) J. Biochem., 99, p. 1191
Wittung-Stafshede, P., (2002) Acc. Chem. Res., 35, p. 201
Garcia-Mira, M.M., Sadqi, M., Fischer, N., Sanchez-Ruiz, J.M., Muñoz, V., (2002) Science, 298, p. 2191
Muñoz, V., (2002) Int. J. Quantum Chem., 90, p. 1522
Robertson, A.D., Murphy, K.P., (1997) Chem. Rev., 97, p. 1251
Farber, P., Darmawan, H., Sprules, T., Mittermaier, A., (2010) J. Am. Chem. Soc., 132, p. 6214
Malgieri, G., Russo, L., Esposito, S., Baglivo, I., Zaccaro, L., Pedone, E.M., Di Blasio, B., Fattorusso, R., (2007) Proc. Natl. Acad. Sci. U.S.A., 104, p. 17341
Baglivo, I., Russo, L., Esposito, S., Malgieri, G., Renda, M., Salluzzo, A., Di Blasio, B., Pedone, P.V., (2009) Proc. Natl. Acad. Sci. U.S.A., 106, p. 6933
Zarrine-Afsar, A., Larson, S.M., Davidson, A.R., (2005) Curr. Opin. Struct. Biol., 15, p. 42
Naganathan, A.N., Li, P., Perez-Jimenez, R., Sanchez-Ruiz, J.M., Muñoz, V., (2010) J. Am. Chem. Soc., 132, p. 11183
Nickson, A.A., Clarke, J., (2010) Methods, 52, p. 38
Nomura, A., Sugiura, Y., (2002) Inorg. Chem., 41, p. 3693
Isernia, C., Bucci, E., Leone, M., Zaccaro, L., Di Lello, P., Digilio, G., Esposito, S., Fattorusso, R., (2003) ChemBioChem, 4, p. 171
Chekmeneva, E., Prohens, R., Díaz-Cruz, J.M., Ariño, C., Esteban, M., (2008) Anal. Biochem., 375, p. 82
Blasie, C.A., Berg, J.M., (2002) Biochemistry, 41, p. 15068
Manetto, G.D., Grasso, D.M., Milardi, D., Pappalardo, M., Guzzi, R., Sportelli, L., Verbeet, M.P., La Rosa, C., (2007) ChemBioChem, 8, p. 1941
La, R.C., Milardi, D., Grasso, D.M., Verbeet, M.P., Canters, G.W., Sportelli, L., Guzzi, R., (2002) Eur. Biophys. J., 30, p. 559
Milardi, D., Arnesano, F., Grasso, G., Magrì, A., Tabbì, G., Scintilla, S., Natile, G., Rizzarelli, E., (2007) Angew. Chem., Int. Ed., 46, p. 7993
Hu, C.Q., Sturtevant, J.M., Thomson, J.A., Erickson, R.E., Pace, C.N., (1992) Biochemistry, 31, p. 4876
Fischer, H., Polikarpov, I., Craievich, A.F., (2004) Protein Sci., 13, p. 2825
Foster, M.P., Wuttke, D.S., Clemens, K.R., Jahnke, W., Radhakrishnan, I., Tennant, L., Reymond, M., Wright, P.E., (1998) J. Biomol. NMR, 12, p. 51
Mori, S., Abeygunawardana, C., Johnson, M.O., Van Zijl, P.C., (1995) J. Magn. Reson., Ser. B, 108, p. 94
Bai, Y., Milne, J.S., Mayne, L., Englander, S.W., (1993) Proteins, 17, p. 75
Zhang, Y.Z., Paterson, Y., Roder, H., (1995) Protein Sci., 4, p. 804
Hvidt, A., Nielsen, S.O., (1966) Adv. Protein Chem., 21, p. 287
Benson, E.E., Linderstrom-Lang, K., (1959) Biochim. Biophys. Acta, 32, p. 579
Berger, A., Linderstrom-Lang, K., (1957) Arch. Biochem. Biophys., 69, p. 106
Bartels, C., Xia, T.H., Billeter, M., Güntert, P., Wüthrich, K., (1995) J. Biomol. NMR, 6, p. 1
Koradi, R., Billeter, M., Wüthrich, K., (1996) J. Mol. Graphics, 14, p. 51
Cohen, D.S., Pielak, G.J., (1994) Protein Sci., 3, p. 1253
Malgieri, G., Zaccaro, L., Leone, M., Bucci, E., Esposito, S., Baglivo, I., Del Gatto, A., Isernia, C., (2011) Biopolymers, 95, p. 801
Rich, A.M., Bombarda, E., Schenk, A.D., Lee, P.E., Cox, E.H., Spuches, A.M., Hudson, L.D., Wilcox, D.E., (2012) J. Am. Chem. Soc., 134, p. 10405
Russo, L., Palmieri, M., Baglivo, I., Esposito, S., Isernia, C., Malgieri, G., Pedone, P.V., Fattorusso, R., (2010) Biomol. NMR Assignments, 4, p. 55
Wishart, D.S., Arndt, D., Berjanskii, M., Tang, P., Zhou, J., Lin, G., (2008) Nucleic Acids Res., 36, p. 496
Freire, E., (1994) Methods Enzymol., 240, p. 502
Muñoz, V., Sanchez-Ruiz, J.M., (2004) Proc. Natl. Acad. Sci. U.S.A., 101, p. 17646
Mizuno, K., Whittaker, M.M., Bächinger, H.P., Whittaker, J.W., (2004) J. Biol. Chem., 279, p. 27339
Huang, F., Sato, S., Sharpe, T.D., Ying, L., Fersht, A.R., (2007) Proc. Natl. Acad. Sci. U.S.A., 104, p. 123
Naganathan, A.N., Sanchez-Ruiz, J.M., Muñoz, V., (2005) J. Am. Chem. Soc., 127, p. 17970
Fung, A., Li, P., Godoy-Ruiz, R., Sanchez-Ruiz, J.M., Muñoz, V., (2008) J. Am. Chem. Soc., 130, p. 7489
Godoy-Ruiz, R., Henry, E.R., Kubelka, J., Hofrichter, J., Muñoz, V., Sanchez-Ruiz, J.M., Eaton, W.A., (2008) J. Phys. Chem. B, 112, p. 5938
Bai, Y., Sosnick, T.R., Mayne, L., Englander, S.W., (1995) Science, 269, p. 192
Englander, S.W., (2000) Annu. Rev. Biophys. Biomol. Struct., 29, p. 213
Wilson, C.J., Apiyo, D., Wittung-Stafshede, P., (2004) Q. Rev. Biophys., 37, p. 285
Chang, S., Jiao, X., Hu, J.P., Chen, Y., Tian, X.H., (2010) Int. J. Mol. Sci., 11, p. 4014
Gopal, S.M., Wenzel, W., (2006) Angew. Chem., Int. Ed., 45, p. 7726
Li, W., Zhang, J., Wang, J., Wang, W., (2008) J. Am. Chem. Soc., 130, p. 892
Miura, T., Satoh, T., Takeuchi, H., (1998) Biochim. Biophys. Acta, 1384, p. 171
Bai, Y., (1999) J. Biomol. NMR, 15, p. 65
Bai, Y., (2006) Chem. Rev., 106, p. 1757
Yi, Q., Baker, D., (1996) Protein Sci., 5, p. 1060
Muñoz, V., Sadqi, M., Naganathan, A.N., De Sancho, D., (2008) HFSP J., 2, p. 342
Sborgi, L., Verma, A., Muñoz, V., De Alba, E., (2011) PLoS One, 6, p. 26409
Cho, S.S., Weinkam, P., Wolynes, P.G., (2008) Proc. Natl. Acad. Sci. U.S.A., 105, p. 118
Bryngelson, J. D., Onuchic, J. N., Socci, N. D., Wolynes, P. G., (1995) Proteins, 21, p. 167
Brockwell, D. J., Radford, S. E., (2007) Curr. Opin. Struct. Biol., 17, p. 30
Korzhnev, D. M., Salvatella, X., Vendruscolo, M., Di Nardo, A. A., Davidson, A. R., Dobson, C. M., Kay, L. E., (2004) Nature, 430, p. 586
Coyne, H. J., Ciofi-Baffoni, S., Banci, L., Bertini, I., Zhang, L., George, G. N., Winge, D. R., (2007) J. Biol. Chem., 282, p. 8926
Garcia-Mira, M. M., Sadqi, M., Fischer, N., Sanchez-Ruiz, J. M., Mu oz, V., (2002) Science, 298, p. 2191
Mu oz, V., (2002) Int. J. Quantum Chem., 90, p. 1522
Robertson, A. D., Murphy, K. P., (1997) Chem. Rev., 97, p. 1251
Naganathan, A. N., Li, P., Perez-Jimenez, R., Sanchez-Ruiz, J. M., Mu oz, V., (2010) J. Am. Chem. Soc., 132, p. 11183
Nickson, A. A., Clarke, J., (2010) Methods, 52, p. 38
Blasie, C. A., Berg, J. M., (2002) Biochemistry, 41, p. 15068
Manetto, G. D., Grasso, D. M., Milardi, D., Pappalardo, M., Guzzi, R., Sportelli, L., Verbeet, M. P., La Rosa, C., (2007) ChemBioChem, 8, p. 1941
La, R. C., Milardi, D., Grasso, D. M., Verbeet, M. P., Canters, G. W., Sportelli, L., Guzzi, R., (2002) Eur. Biophys. J., 30, p. 559
Hu, C. Q., Sturtevant, J. M., Thomson, J. A., Erickson, R. E., Pace, C. N., (1992) Biochemistry, 31, p. 4876
Foster, M. P., Wuttke, D. S., Clemens, K. R., Jahnke, W., Radhakrishnan, I., Tennant, L., Reymond, M., Wright, P. E., (1998) J. Biomol. NMR, 12, p. 51
Bai, Y., Milne, J. S., Mayne, L., Englander, S. W., (1993) Proteins, 17, p. 75
Zhang, Y. Z., Paterson, Y., Roder, H., (1995) Protein Sci., 4, p. 804
Benson, E. E., Linderstrom-Lang, K., (1959) Biochim. Biophys. Acta, 32, p. 579
Cohen, D. S., Pielak, G. J., (1994) Protein Sci., 3, p. 1253
Rich, A. M., Bombarda, E., Schenk, A. D., Lee, P. E., Cox, E. H., Spuches, A. M., Hudson, L. D., Wilcox, D. E., (2012) J. Am. Chem. Soc., 134, p. 10405
Wishart, D. S., Arndt, D., Berjanskii, M., Tang, P., Zhou, J., Lin, G., (2008) Nucleic Acids Res., 36, p. 496
Mu oz, V., Sanchez-Ruiz, J. M., (2004) Proc. Natl. Acad. Sci. U. S. A., 101, p. 17646
Englander, S. W., (2000) Annu. Rev. Biophys. Biomol. Struct., 29, p. 213
Wilson, C. J., Apiyo, D., Wittung-Stafshede, P., (2004) Q. Rev. Biophys., 37, p. 285
Gopal, S. M., Wenzel, W., (2006) Angew. Chem., Int. Ed., 45, p. 7726
Mu oz, V., Sadqi, M., Naganathan, A. N., De Sancho, D., (2008) HFSP J., 2, p. 342
Cho, S. S., Weinkam, P., Wolynes, P. G., (2008) Proc. Natl. Acad. Sci. U. S. A., 105, p. 118
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2013 Apr 2; 135(13): 5220-5228.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 11.444, 5-year impact factor: 11.015
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84875797582&partnerID=40&md5=265e8956facb9aafd785c05d92042914
Keywords: Biological Process, Homologous Proteins, Intermediate State, Protein Folding Reaction, Protein Misfolding, Structural Feature, Thermal Unfolding, Zinc Finger Domains, Metal Ions, Random Processes, Thermodynamics, Zinc Compounds, Zinc Finger Protein, Article, Circular Dichroism, Differential Scanning Calorimetry, Molecular Mechanics, Nonhuman, Nuclear Magnetic Resonance, Prokaryotic Cell, Protein Structure, Magnetic Resonance Spectroscopy, Models,
Affiliations:
*** IBB - CNR ***
Department of Environmental, Biological and Pharmaceutical Science and Technology, Second University of Naples, Via Vivaldi 43, 81100 Caserta, Italy
Institute of Biostructures and Bioimaging-CNR (Naples), Via Mezzocannone 16, 80134 Naples, Italy
References:
Tanford, C., (1968) Adv. Protein Chem., 23, p. 12
Bryngelson, J.D., Onuchic, J.N., Socci, N.D., Wolynes, P.G., (1995) Proteins, 21, p. 167
Halskau, O., Perez-Jimenez, R., Ibarra-Molero, B., Underhaug, J., Muñoz, V., Martinez, A., Sanchez-Ruiz, J.M., (2008) Proc. Natl. Acad. Sci. U.S.A., 105, p. 8625
Sadqi, M., Fushman, D., Muñoz, V., (2006) Nature, 442, p. 317
Brockwell, D.J., Radford, S.E., (2007) Curr. Opin. Struct. Biol., 17, p. 30
Korzhnev, D.M., Salvatella, X., Vendruscolo, M., Di Nardo, A.A., Davidson, A.R., Dobson, C.M., Kay, L.E., (2004) Nature, 430, p. 586
Chen, Y., Ding, F., Nie, H., Serohijos, A.W., Sharma, S., Wilcox, K.C., Yin, S., Dokholyan, N.V., (2008) Arch. Biochem. Biophys., 469, p. 4
Coyne, H.J., Ciofi-Baffoni, S., Banci, L., Bertini, I., Zhang, L., George, G.N., Winge, D.R., (2007) J. Biol. Chem., 282, p. 8926
Ikeguchi, M., Kuwajima, K., Sugai, S., (1986) J. Biochem., 99, p. 1191
Wittung-Stafshede, P., (2002) Acc. Chem. Res., 35, p. 201
Garcia-Mira, M.M., Sadqi, M., Fischer, N., Sanchez-Ruiz, J.M., Muñoz, V., (2002) Science, 298, p. 2191
Muñoz, V., (2002) Int. J. Quantum Chem., 90, p. 1522
Robertson, A.D., Murphy, K.P., (1997) Chem. Rev., 97, p. 1251
Farber, P., Darmawan, H., Sprules, T., Mittermaier, A., (2010) J. Am. Chem. Soc., 132, p. 6214
Malgieri, G., Russo, L., Esposito, S., Baglivo, I., Zaccaro, L., Pedone, E.M., Di Blasio, B., Fattorusso, R., (2007) Proc. Natl. Acad. Sci. U.S.A., 104, p. 17341
Baglivo, I., Russo, L., Esposito, S., Malgieri, G., Renda, M., Salluzzo, A., Di Blasio, B., Pedone, P.V., (2009) Proc. Natl. Acad. Sci. U.S.A., 106, p. 6933
Zarrine-Afsar, A., Larson, S.M., Davidson, A.R., (2005) Curr. Opin. Struct. Biol., 15, p. 42
Naganathan, A.N., Li, P., Perez-Jimenez, R., Sanchez-Ruiz, J.M., Muñoz, V., (2010) J. Am. Chem. Soc., 132, p. 11183
Nickson, A.A., Clarke, J., (2010) Methods, 52, p. 38
Nomura, A., Sugiura, Y., (2002) Inorg. Chem., 41, p. 3693
Isernia, C., Bucci, E., Leone, M., Zaccaro, L., Di Lello, P., Digilio, G., Esposito, S., Fattorusso, R., (2003) ChemBioChem, 4, p. 171
Chekmeneva, E., Prohens, R., Díaz-Cruz, J.M., Ariño, C., Esteban, M., (2008) Anal. Biochem., 375, p. 82
Blasie, C.A., Berg, J.M., (2002) Biochemistry, 41, p. 15068
Manetto, G.D., Grasso, D.M., Milardi, D., Pappalardo, M., Guzzi, R., Sportelli, L., Verbeet, M.P., La Rosa, C., (2007) ChemBioChem, 8, p. 1941
La, R.C., Milardi, D., Grasso, D.M., Verbeet, M.P., Canters, G.W., Sportelli, L., Guzzi, R., (2002) Eur. Biophys. J., 30, p. 559
Milardi, D., Arnesano, F., Grasso, G., Magrì, A., Tabbì, G., Scintilla, S., Natile, G., Rizzarelli, E., (2007) Angew. Chem., Int. Ed., 46, p. 7993
Hu, C.Q., Sturtevant, J.M., Thomson, J.A., Erickson, R.E., Pace, C.N., (1992) Biochemistry, 31, p. 4876
Fischer, H., Polikarpov, I., Craievich, A.F., (2004) Protein Sci., 13, p. 2825
Foster, M.P., Wuttke, D.S., Clemens, K.R., Jahnke, W., Radhakrishnan, I., Tennant, L., Reymond, M., Wright, P.E., (1998) J. Biomol. NMR, 12, p. 51
Mori, S., Abeygunawardana, C., Johnson, M.O., Van Zijl, P.C., (1995) J. Magn. Reson., Ser. B, 108, p. 94
Bai, Y., Milne, J.S., Mayne, L., Englander, S.W., (1993) Proteins, 17, p. 75
Zhang, Y.Z., Paterson, Y., Roder, H., (1995) Protein Sci., 4, p. 804
Hvidt, A., Nielsen, S.O., (1966) Adv. Protein Chem., 21, p. 287
Benson, E.E., Linderstrom-Lang, K., (1959) Biochim. Biophys. Acta, 32, p. 579
Berger, A., Linderstrom-Lang, K., (1957) Arch. Biochem. Biophys., 69, p. 106
Bartels, C., Xia, T.H., Billeter, M., Güntert, P., Wüthrich, K., (1995) J. Biomol. NMR, 6, p. 1
Koradi, R., Billeter, M., Wüthrich, K., (1996) J. Mol. Graphics, 14, p. 51
Cohen, D.S., Pielak, G.J., (1994) Protein Sci., 3, p. 1253
Malgieri, G., Zaccaro, L., Leone, M., Bucci, E., Esposito, S., Baglivo, I., Del Gatto, A., Isernia, C., (2011) Biopolymers, 95, p. 801
Rich, A.M., Bombarda, E., Schenk, A.D., Lee, P.E., Cox, E.H., Spuches, A.M., Hudson, L.D., Wilcox, D.E., (2012) J. Am. Chem. Soc., 134, p. 10405
Russo, L., Palmieri, M., Baglivo, I., Esposito, S., Isernia, C., Malgieri, G., Pedone, P.V., Fattorusso, R., (2010) Biomol. NMR Assignments, 4, p. 55
Wishart, D.S., Arndt, D., Berjanskii, M., Tang, P., Zhou, J., Lin, G., (2008) Nucleic Acids Res., 36, p. 496
Freire, E., (1994) Methods Enzymol., 240, p. 502
Muñoz, V., Sanchez-Ruiz, J.M., (2004) Proc. Natl. Acad. Sci. U.S.A., 101, p. 17646
Mizuno, K., Whittaker, M.M., Bächinger, H.P., Whittaker, J.W., (2004) J. Biol. Chem., 279, p. 27339
Huang, F., Sato, S., Sharpe, T.D., Ying, L., Fersht, A.R., (2007) Proc. Natl. Acad. Sci. U.S.A., 104, p. 123
Naganathan, A.N., Sanchez-Ruiz, J.M., Muñoz, V., (2005) J. Am. Chem. Soc., 127, p. 17970
Fung, A., Li, P., Godoy-Ruiz, R., Sanchez-Ruiz, J.M., Muñoz, V., (2008) J. Am. Chem. Soc., 130, p. 7489
Godoy-Ruiz, R., Henry, E.R., Kubelka, J., Hofrichter, J., Muñoz, V., Sanchez-Ruiz, J.M., Eaton, W.A., (2008) J. Phys. Chem. B, 112, p. 5938
Bai, Y., Sosnick, T.R., Mayne, L., Englander, S.W., (1995) Science, 269, p. 192
Englander, S.W., (2000) Annu. Rev. Biophys. Biomol. Struct., 29, p. 213
Wilson, C.J., Apiyo, D., Wittung-Stafshede, P., (2004) Q. Rev. Biophys., 37, p. 285
Chang, S., Jiao, X., Hu, J.P., Chen, Y., Tian, X.H., (2010) Int. J. Mol. Sci., 11, p. 4014
Gopal, S.M., Wenzel, W., (2006) Angew. Chem., Int. Ed., 45, p. 7726
Li, W., Zhang, J., Wang, J., Wang, W., (2008) J. Am. Chem. Soc., 130, p. 892
Miura, T., Satoh, T., Takeuchi, H., (1998) Biochim. Biophys. Acta, 1384, p. 171
Bai, Y., (1999) J. Biomol. NMR, 15, p. 65
Bai, Y., (2006) Chem. Rev., 106, p. 1757
Yi, Q., Baker, D., (1996) Protein Sci., 5, p. 1060
Muñoz, V., Sadqi, M., Naganathan, A.N., De Sancho, D., (2008) HFSP J., 2, p. 342
Sborgi, L., Verma, A., Muñoz, V., De Alba, E., (2011) PLoS One, 6, p. 26409
Cho, S.S., Weinkam, P., Wolynes, P.G., (2008) Proc. Natl. Acad. Sci. U.S.A., 105, p. 118
Bryngelson, J. D., Onuchic, J. N., Socci, N. D., Wolynes, P. G., (1995) Proteins, 21, p. 167
Brockwell, D. J., Radford, S. E., (2007) Curr. Opin. Struct. Biol., 17, p. 30
Korzhnev, D. M., Salvatella, X., Vendruscolo, M., Di Nardo, A. A., Davidson, A. R., Dobson, C. M., Kay, L. E., (2004) Nature, 430, p. 586
Coyne, H. J., Ciofi-Baffoni, S., Banci, L., Bertini, I., Zhang, L., George, G. N., Winge, D. R., (2007) J. Biol. Chem., 282, p. 8926
Garcia-Mira, M. M., Sadqi, M., Fischer, N., Sanchez-Ruiz, J. M., Mu oz, V., (2002) Science, 298, p. 2191
Mu oz, V., (2002) Int. J. Quantum Chem., 90, p. 1522
Robertson, A. D., Murphy, K. P., (1997) Chem. Rev., 97, p. 1251
Naganathan, A. N., Li, P., Perez-Jimenez, R., Sanchez-Ruiz, J. M., Mu oz, V., (2010) J. Am. Chem. Soc., 132, p. 11183
Nickson, A. A., Clarke, J., (2010) Methods, 52, p. 38
Blasie, C. A., Berg, J. M., (2002) Biochemistry, 41, p. 15068
Manetto, G. D., Grasso, D. M., Milardi, D., Pappalardo, M., Guzzi, R., Sportelli, L., Verbeet, M. P., La Rosa, C., (2007) ChemBioChem, 8, p. 1941
La, R. C., Milardi, D., Grasso, D. M., Verbeet, M. P., Canters, G. W., Sportelli, L., Guzzi, R., (2002) Eur. Biophys. J., 30, p. 559
Hu, C. Q., Sturtevant, J. M., Thomson, J. A., Erickson, R. E., Pace, C. N., (1992) Biochemistry, 31, p. 4876
Foster, M. P., Wuttke, D. S., Clemens, K. R., Jahnke, W., Radhakrishnan, I., Tennant, L., Reymond, M., Wright, P. E., (1998) J. Biomol. NMR, 12, p. 51
Bai, Y., Milne, J. S., Mayne, L., Englander, S. W., (1993) Proteins, 17, p. 75
Zhang, Y. Z., Paterson, Y., Roder, H., (1995) Protein Sci., 4, p. 804
Benson, E. E., Linderstrom-Lang, K., (1959) Biochim. Biophys. Acta, 32, p. 579
Cohen, D. S., Pielak, G. J., (1994) Protein Sci., 3, p. 1253
Rich, A. M., Bombarda, E., Schenk, A. D., Lee, P. E., Cox, E. H., Spuches, A. M., Hudson, L. D., Wilcox, D. E., (2012) J. Am. Chem. Soc., 134, p. 10405
Wishart, D. S., Arndt, D., Berjanskii, M., Tang, P., Zhou, J., Lin, G., (2008) Nucleic Acids Res., 36, p. 496
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Structural Zn(II) Implies a Switch from Fully Cooperative to Partly Downhill Folding in Highly Homologous Proteins
In the funneled landscape, proteins fold to their native states through a stochastic process in which the free energy decreases spontaneously and unfolded, transition, native, and possible intermediate states correspond to local minima or saddle points. Atomic description of the folding pathway appears therefore to be essential for a deep comprehension of the folding mechanism. In metallo-proteins, characterization of the folding pathways becomes even more complex, and therefore, despite their fundamental role in critical biological processes, little is known about their folding and assembly. The study of the mechanisms through which a cofactor influences the protein folding/unfolding reaction has been the rationale of the present study aimed at contributing to the search for cofactors' general roles in protein folding reactions. In particular, we have investigated the folding pathway of two homologous proteins, Ros87, which contains a prokaryotic zinc finger domain, and Ml4(52-151), lacking the zinc ion. Using a combination of CD, DSC and NMR techniques, we determined the thermodynamics and the structural features, at an atomic level, of the thermal unfolding of Ros87 and compared them to the behavior of Ml4(52-151). Our results, also corroborated by NMR H-1/H-2 exchange measurements, show that the presence of the structural Zn(II) in Ros87 implies a switch from the Ml4(52-151), fully cooperative to a two-step unfolding process in which the intermediate converts to the native state through a downhill barrierless transition. This observation, which has never been reported for any metal ion so far, may have a significant role in the understanding of the protein misfolding associated with the presence of metal ions, as observed in neurodegenerative diseases.
In the funneled landscape, proteins fold to their native states through a stochastic process in which the free energy decreases spontaneously and unfolded, transition, native, and possible intermediate states correspond to local minima or saddle points. Atomic description of the folding pathway appears therefore to be essential for a deep comprehension of the folding mechanism. In metallo-proteins, characterization of the folding pathways becomes even more complex, and therefore, despite their fundamental role in critical biological processes, little is known about their folding and assembly. The study of the mechanisms through which a cofactor influences the protein folding/unfolding reaction has been the rationale of the present study aimed at contributing to the search for cofactors' general roles in protein folding reactions. In particular, we have investigated the folding pathway of two homologous proteins, Ros87, which contains a prokaryotic zinc finger domain, and Ml4(52-151), lacking the zinc ion. Using a combination of CD, DSC and NMR techniques, we determined the thermodynamics and the structural features, at an atomic level, of the thermal unfolding of Ros87 and compared them to the behavior of Ml4(52-151). Our results, also corroborated by NMR H-1/H-2 exchange measurements, show that the presence of the structural Zn(II) in Ros87 implies a switch from the Ml4(52-151), fully cooperative to a two-step unfolding process in which the intermediate converts to the native state through a downhill barrierless transition. This observation, which has never been reported for any metal ion so far, may have a significant role in the understanding of the protein misfolding associated with the presence of metal ions, as observed in neurodegenerative diseases.
Structural Zn(II) Implies a Switch from Fully Cooperative to Partly Downhill Folding in Highly Homologous Proteins
Structural Zn(II) Implies a Switch from Fully Cooperative to Partly Downhill Folding in Highly Homologous Proteins
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Benetti F, Biarnes X, Attanasio F, Rizzarelli E, Laio A, Legname G
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Palladino P, Ronga L, Tizzano B, Rossi F, Ragone R, Tancredi T, Saviano G, Facchiano A, Costantini S, Ruvo M, Benedetti E
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* Topology Controls the Electronic Absorption and Delocalization of Electron Holes in Guanine Quadruplexes (307 views)
Chemistry (ISSN: 1521-3765electronic, 0947-6539linking), 2018 Oct 12; 24(57): 15185-15189.
Impact Factor: 5.476
View Export to BibTeX Export to EndNote
Malgieri G, D'Abrosca G, Pirone L, Toto A, Palmieri M, Russo L, Sciacca MFM, Tate R, Sivo V, Baglivo I, Majewska R, Coletta M, Pedone PV, Isernia C, De Stefano M, Gianni S, Pedone EM, Milardi D, Fattorusso R
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Chem Sci (ISSN: 2041-6520linking, 2041-6520print, 2041-6539), 2018 Apr 7; 9(13): 3290-3298.
Impact Factor: 9.063
View Export to BibTeX Export to EndNote
Benetti F, Biarnés X, Attanasio F, Giachin G, Rizzarelli E, Legname G
* Structural determinants in prion protein folding and stability (554 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 0022-2836linking), 2014 Nov 11; 426(22): 3796-3810.
Impact Factor: 4.333
View Export to BibTeX Export to EndNote
Oliveri V, Attanasio F, Puglisi A, Spencer J, Sgarlata C, Vecchio G
* Multifunctional 8-hydroxyquinoline-appended cyclodextrins as new inhibitors of metal-induced protein aggregation (619 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2014 Jul 14; 20(29): 8954-8964.
Impact Factor: 5.731
View Export to BibTeX Export to EndNote
Pica A, Russo Krauss I, Castellano I, Rossi M, La Cara F, Graziano G, Sica F, Merlino A
* Exploring The Unfolding Mechanism Of Gamma-Glutamyltranspeptidases: The Case Of The Thermophilic Enzyme From Geobacillus Thermodenitrificans (396 views)
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Impact Factor: 3.733
View Export to BibTeX Export to EndNote
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* Description and Characterization of a Highly Stable Enthalpic Intermediate State in Mouse Prion Protein Folding (306 views)
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Impact Factor: 2.85
View Export to BibTeX Export to EndNote
Ponticelli S, Marasco D, Tarallo V, Albuquerque RJC, Mitola S, Takeda A, Stassen J, Presta M, Ambati J, Ruvo M, De Falco S
* Modulation of Angiogenesis by a Tetrameric Tripeptide That Antagonizes Vascular Endothelial Growth Factor Receptor (536 views)
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Impact Factor: 5.52
View Export to BibTeX Export to EndNote
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Understanding Biology Using Peptides, 2006; N/D: N/D-N/D.
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8 Records (6 excluding Abstracts).
Total impact factor: 39.32 (33.856 excluding Abstracts).
Total 5 year impact factor: 37.669 (32.134 excluding Abstracts).
Total impact factor: 39.32 (33.856 excluding Abstracts).
Total 5 year impact factor: 37.669 (32.134 excluding Abstracts).
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