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 Thermodynamics Of Azurin Folding: The Role Of The Copper Ion (87 visite) Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2008 Sep; 93(2): 575-581. Tipo di articolo: Journal Article, , Impact factor: 1.63, Impact factor a 5 anni: 1.473, Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-48349125685&partnerID=40&md5=fc1f0ad9fcf318f2d1c087297eedb5d0 Parole chiave: Apo-Azurin, Binding, Folding Gibbs Free Energy, Lumry-Eyring Models, Stability, Copper, Differential Scanning Calorimetry, Dynamics, Ions, Laser Interferometry, Metal Ions, Protein Folding, Pyrolysis, Thermodynamics, Copper (ii) Ions, Differential Scanning Calorimetry (photo-Dsc), Thermodynamic Stability, Copper(ii) Ions, Affiliazioni: *** IBB - CNR *** Dipartimento di Scienze Chimiche, Universit di Catania, V. le A. Doria 6, Catania 95125, Italy Istituto di Biostrutture e Bioimmagini, CNR, Sezione di Catania, Viale Andrea Doria 6, Catania 95125, Italy Riferimenti: Engeseth, H. R., McMillin, D. R., (1986) Biochemistry, 25, p. 244 Surewicz, W. K., Szabo, A. G., Mantsch, H. H., (1987) Eur. J. Biochem., 167, p. 519 Kroes, S. J., Canters, G. W., Gilardi, G., Van Hoek, A., Visser, A. J., (1998) Biophys. J., 75, p. 2441 Murphy, M. E. P., Lindley, P. F., Adman, E. T., (1997) Protein Sci., 6, p. 761 Leckner, J., Bonander, N., Wittung-Stafshede, P., Malmstrom, B. G., Karlsson, B. G., (1997) Biochim. Biophys. Acta, 1342, p. 19 Sciacca, M. F. M., Milardi, D., Pappalardo, M., La Rosa, C., Grasso, D. M., (2006) J. Therm. Anal. Cal., 86, p. 303 Solomon, E. I., Baldwin, M. J., Lowery, M., (1992) Chem Rev., 92, p. 521 Adman, E. T., Jensen, L. H., (1981) Isr. J. Chem., 21, p. 8 Nar, H., Messerschmidt, A., Huber, R., Van De Kamp, M., Canters, G. W., (1991) J. Mol. Biol., 221, p. 765 Adman, E. T., (1991) Adv. Protein Chem., 42, p. 144 La Rosa, C., Milardi, D., Grasso, D., (1998) Recent Res. Devel. in Phys. Chem., 2, p. 175 Bonander, N., Karlsson, B. G., V nng rd, T., (1995) Biochim. Biophys. Acta, 1251, p. 48 Guzzi, R., Sportelli, L., La Rosa, C., Milardi, D., Grasso, D., Ph., V. M., Canters, G. W., (1999) Biophys. J., 77, p. 1052 Bonander, N., Leckner, J., Guo, H., Karlsson, B. G., Sjolin, L., (2000) Eur. J. Biochem., 267, p. 4511 Pozdnyakova, Guidry, J., Wittung-Stafshede, P., (2000) J. Am. Chem. Soc., 122, p. 6337 Van De Kamp, M., Hali, F. C., Rosato, N., Finazzi-Agr, A., Canters, G. W., (1990) Biochim. Biophys. Acta, 1019, p. 283 Moratal, J. M., Romero, A., Salgado, J., Perales-Alarc n, A., Jim nez, H. R., (1995) Eur. J. Biochem., 228, p. 653 Privalov, P. L., Gill, S. J., (1988) Adv. Protein Chem., 39, p. 191 Sanchez-Ruiz, J. M., Lopez-Lacomba, J. L., Cortijo, M., Mateo, P. L., (1988) Biochemistry, 27, p. 1648 Milardi, D., La Rosa, C., Grasso, D., (1994) Biophys. Chem., 52, p. 183 Manetto, G. D., La Rosa, C., Milardi, D., Grasso, D. M., (2005) J. Therm. Anal. Cal., 80, p. 263 Freire, E., Van Odsol, W., Mayorga, O. L., Sanchez-Ruiz, J. M., (1990) Annu. Rev. Biophys. Biophys., Chem, 19, p. 159 Murphy, P. K., Gill, S. J., (1991) J. Mol. Biol., 222, p. 699 Privalov, P. L., Creighton, T. E., (1992) Protein Folding, pp. 83-126. , W. H. Freeman and Co. New York Bevington, P. R., (1969) Data Reduction and Error Analysis for the Physical Sciences, , McGraw-Hill Book Company New York Pozdnyakova, I., Guidry, J., Wittung-Stafshede, P., (2001) Arch. Biochem. Biophys., 390, p. 146 Smith, R. M., Martell, A. E., (1989) Critical Stability Constants: Volume 6 Second Supplement, , Plenum Press New York and London Kodama, M., Ebine, H., Volume 3: Other organic ligands (1967) Bull. Chem. Soc. Jpn., 40, p. 1857 Engeseth, H.R., McMillin, D.R., (1986) Biochemistry, 25, p. 244 Surewicz, W.K., Szabo, A.G., Mantsch, H.H., (1987) Eur. J. Biochem., 167, p. 519 Kroes, S.J., Canters, G.W., Gilardi, G., Van Hoek, A., Visser, A.J., (1998) Biophys. J., 75, p. 2441 Murphy, M.E.P., Lindley, P.F., Adman, E.T., (1997) Protein Sci., 6, p. 761 Sciacca, M.F.M., Milardi, D., Pappalardo, M., La Rosa, C., Grasso, D.M., (2006) J. Therm. Anal. Cal., 86, p. 303 Solomon, E.I., Baldwin, M.J., Lowery, M., (1992) Chem Rev., 92, p. 521 Adman, E.T., Jensen, L.H., (1981) Isr. J. Chem., 21, p. 8 Adman, E.T., (1991) Adv. Protein Chem., 42, p. 144 Moratal, J.M., Romero, A., Salgado, J., Perales-Alarcòn, A., Jiménez, H.R., (1995) Eur. J. Biochem., 228, p. 653 Privalov, P.L., Gill, S.J., (1988) Adv. Protein Chem., 39, p. 191 Sanchez-Ruiz, J.M., Lopez-Lacomba, J.L., Cortijo, M., Mateo, P.L., (1988) Biochemistry, 27, p. 1648 Manetto, G.D., La Rosa, C., Milardi, D., Grasso, D.M., (2005) J. Therm. Anal. Cal., 80, p. 263 Murphy, P.K., Gill, S.J., (1991) J. Mol. Biol., 222, p. 699 Privalov, P.L., Creighton, T.E., (1992) Protein Folding, pp. 83-126. , W. H. Freeman and Co. New York Bevington, P.R., (1969) Data Reduction and Error Analysis for the Physical Sciences, , McGraw-Hill Book Company New York Smith, R.M., Martell, A.E., (1989) Critical Stability Constants: Volume 6 Second Supplement, , Plenum Press New York and London The role played by the metal ion in thermodynamics of azurin folding was addressed by studying the thermal denaturation of the apo-form by differential scanning calorimetry (DSC), and by comparing the results with data concerning the holo protein. The thermal unfolding experiments showed that at 25 C the presence of metal ion increases the thermodynamic stability of azurin by 24 kJ mol-1. A comparison between the unfolding and the copper binding free energies allow us to assert that the unfolded polypeptide chain binds copper and subsequently folds into native holo azurin, being this the thermodynamically most favourable process in driving azurin folding. 2008 Springer Science+Business Media, LLC
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Impact Factor: 1.438 Dettagli Esporta in BibTeX Esporta in EndNote Granata V, Palladino P, Tizzano B, Negro A, Berisio R, Zagari A * The effect of the osmolyte trimethylamine N-oxide on the stability of the prion protein at low pH (79 visite) Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2006 Jun 15; 82(3): 234-240. Impact Factor: 2.48 Dettagli Esporta in BibTeX Esporta in EndNote Palladino P, Ronga L, Tizzano B, Rossi F, Ragone R, Tancredi T, Saviano G, Facchiano A, Costantini S, Ruvo M, Benedetti E * Prion protein misfolding: Conformational stability of the alpha 2-helix (84 visite) Understanding Biology Using Peptides, 2006; N/D: N/D-N/D. Impact Factor: 2.614 Dettagli Esporta in BibTeX Esporta in EndNote Di Natale G, Grasso G, Impellizzeri G, La Mendola D, Micera G, Mihala N, Nagy Z, Osz K, Pappalardo G, Rigó V, Rizzarelli E, Sanna D, Sóvágó I * Copper(II) interaction with unstructured prion domain outside the octarepeat region: Speciation, stability, and binding details of copper(II) complexes with PrP106-126 peptides (141 visite) Inorg Chem (ISSN: 0020-1669, 1520-510x, 1520-510xelectronic), 2005 Oct 3; 44(20): 7214-7225. Impact Factor: 3.851 Dettagli Esporta in BibTeX Esporta in EndNote Bucci E, Vitagliano L, Barone R, Sorrentino S, D'Alessio G, Graziano G * On the thermal stability of the two dimeric forms of ribonuclease (93 visite) Biophysical Chemistry (ISSN: 0301-4622), 2005 Jul 1; 116(2): 89-95. Impact Factor: 1.925 Dettagli Esporta in BibTeX Esporta in EndNote De Simone A, Dodson GG, Verma CS, Zagari A, Fraternali F * Prion And Water: Tight And Dynamical Hydration Sites Have A Key Role In Structural Stability (63 visite) Proceedings Of The National Academy Of Sciences Of The United States Of America, 2005; 102: 7535-7540. Impact Factor: 0 Dettagli Esporta in BibTeX Esporta in EndNote Merlino A, Graziano G, Mazzarella L * Structural And Dynamic Effects Of Alpha-Helix Deletion In Sso7d: Implications For Protein Thermal Stability (99 visite) Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2004 Dec 1; 57(4): 692-701. Impact Factor: 4.429 Dettagli Esporta in BibTeX Esporta in EndNote Sica F, Di Fiore A, Merlino A, Mazzarella L * Structure and stability of the non-covalent swapped dimer of bovine seminal ribonuclease - An enzyme tailored to evade ribonuclease protein inhibitor (113 visite) J Biol Chem Journal Of Biological Chemistry (ISSN: 0021-9258, 1083-351x), 2004 Sep 27; 279(35): 36753-36760. Impact Factor: 6.355 Dettagli Esporta in BibTeX Esporta in EndNote Berisio R, Granata V, Vitagliano L, Zagari A * Imino acids and collagen triple helix stability: Characterization of collagen-like polypeptides containing Hyp-Hyp-Gly sequence repeats (132 visite) J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2004 Sep 22; 126(37): 11402-11403. Impact Factor: 6.903 Dettagli Esporta in BibTeX Esporta in EndNote Pappalardo M, Milardi D, La Rosa C, Zannoni C, Rizzarelli E, Grasso D * A molecular dynamics study on the conformational stability of PrP 180-193 helix II prion fragment (113 visite) Chemical Physics Letters (ISSN: 0009-2614), 2004 Jun 1; 390(4-6): 511-516. Impact Factor: 2.438 Dettagli Esporta in BibTeX Esporta in EndNote Leone M, Di Lello P, Ohlenschläger O, Pedone E, Bartolucci S, Rossi M, Di Blasio B, Pedone C, Saviano M, Isernia C, Fattorusso R * Solution structure and backbone dynamics of the K18G/R82E Alicyclobacillus acidocaldarius thioredoxin mutant: A molecular analysis of its reduced thermal stability (100 visite) Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2004 May 25; 43(20): 6043-6058. Impact Factor: 4.008 Dettagli Esporta in BibTeX Esporta in EndNote Berisio R, Granata V, Vitagliano L, Zagari A * Characterization of Collagen-Like Heterotrimers: Implications for Triple-Helix Stability (116 visite) Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004 Apr 15; 73(6): 682-688. Impact Factor: 2.863 Dettagli Esporta in BibTeX Esporta in EndNote Pedone E, Bartolucci S, Rossi M, Pierfederici FM, Scire A, Cacciamani T, Tanfani F * Structural and thermal stability analysis of Escherichia coli and Alicyclobacillus acidocaldarius thioredoxin revealed a molten globule-like state in thermal denaturation pathway of the proteins: an infrared spectroscopic study (141 visite) Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2003 Sep 1; 373: 875-883. Impact Factor: 4.101 Dettagli Esporta in BibTeX Esporta in EndNote Bartolucci S, De Simone G, Galdiero S, Improta R, Menchise V, Pedone C, Pedone E, Saviano M * An integrated structural and computational study of the thermostability of two thioredoxin mutants from Alicyclobacillus acidocaldarius (105 visite) J Bacteriol Journal Of Bacteriology (ISSN: 0021-9193, 1098-5530), 2003 Jul; 185(14): 4285-4289. Impact Factor: 4.175 Dettagli Esporta in BibTeX Esporta in EndNote Milardi D, Grasso DM, Verbeet MP, Canters GW, La Rosa C * Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: Synergism among multiple depletions (119 visite) Arch Biochem Biophys (ISSN: 0003-9861), 2003 Jun 1; 414(1): 121-127. Impact Factor: 2.338 Dettagli Esporta in BibTeX Esporta in EndNote Tabbì G, Cassino C, Cavigiolio G, Colangelo D, Ghiglia A, Viano I, Osella D * Water stability and cytotoxic activity relationship of a series of ferrocenium derivatives. ESR insights on the radical production during the degradation process (126 visite) J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2002 Dec 19; 45(26): 5786-5796. Impact Factor: 4.566 Dettagli Esporta in BibTeX Esporta in EndNote Improta R, Mele F, Crescenzi O, Benzi C, Barone V * Understanding the role of stereoelectronic effects in determining collagen stability. 2. A quantum mechanical/molecular mechanical study of (Proline-Proline-Glycine)n polypeptides (115 visite) J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2002 Jul 3; 124(26): 7857-7865. Impact Factor: 6.201 Dettagli Esporta in BibTeX Esporta in EndNote Berisio R, Vitagliano L, Mazzarella L, Zagari A * Recent progress on collagen triple helix structure, stability and assembly (94 visite) Protein And Peptide Letters (ISSN: 0929-8665, 1875-5305), 2002 Apr; 9(2): 107-116. Impact Factor: 0.622 Dettagli Esporta in BibTeX Esporta in EndNote Vitagliano L, Berisio R, Mastrangelo A, Mazzarella L, Zagari A * Preferred proline puckerings in cis and trans peptide groups: Implications for collagen stability (107 visite) Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2001 Dec; 10(12): 2627-2632. Impact Factor: 3.472 Dettagli Esporta in BibTeX Esporta in EndNote Ritieni A, Monti SM, Moretti A, Randazzo G, Ferracane R, Fogliano V Stability Of Fusaproliferin, A Mycotoxin From Fusarium (92 visite) J Sci Food Agric, 1999; 79: 1676-1680. Impact Factor: 0 Dettagli Esporta in BibTeX Esporta in EndNote 64 Records (61 escludendo Abstract e Conferenze). Impact factor totale: 227.435 (220.699 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 240.705 (233.541 escludendo Abstract e Conferenze). Esporta in BibTeX Esporta in EndNote Ultima modifica di Marco Comerci in data Thursday 19 March 2015, 12:58:02 87 visite. 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