Thermodynamics Of Azurin Folding: The Role Of The Copper Ion (333 views)
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2008 Sep; 93(2): 575-581.
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Paper type: Journal Article,
Impact factor: 1.63, 5-year impact factor: 1.473
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-48349125685&partnerID=40&md5=fc1f0ad9fcf318f2d1c087297eedb5d0
Keywords: 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,
Affiliations:
*** 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
References:
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
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2008 Sep; 93(2): 575-581.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 1.63, 5-year impact factor: 1.473
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-48349125685&partnerID=40&md5=fc1f0ad9fcf318f2d1c087297eedb5d0
Keywords: 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,
Affiliations:
*** 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
References:
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
Thermodynamics Of Azurin Folding: The Role Of The Copper Ion
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
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
Thermodynamics Of Azurin Folding: The Role Of The Copper Ion
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Thermodynamics Of Azurin Folding: The Role Of The Copper Ion
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Smaldone G, Vigorita M, Ruggiero A, Balasco N, Dattelbaum JD, D'Auria S, Del Vecchio P, Graziano G, Vitagliano L
* Proline 235 plays a key role in the regulation of the oligomeric states of Thermotoga maritima Arginine Binding Protein (314 views)
Bba-Gen Subjects (ISSN: 0005-2728, 0006-3002print, 1570-9639print), 2016 Jul; 1864(7): 814-824.
Impact Factor: 4.932
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Nicastro MC, Spigolon D, Librizzi F, Moran O, Ortore MG, Bulone D, Biagio PLS, Carrotta R
* Amyloid β-peptide insertion in liposomes containing GM1-cholesterol domains (367 views)
Biophys Chem (ISSN: 0301-4622, 0301-4622linking), 2016; 208: 9-16.
Impact Factor: 2.402
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Berisio R, Squeglia F, Ruggiero A, Petraccone L, Stellato MI, Del Vecchio P
* Differential thermodynamic behaviours of the extra-cellular regions of two Ser/Thr PrkC kinases revealed by calorimetric studies (438 views)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2015 Feb 8; 1854(5): 402-409.
Impact Factor: 5.158
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Romanucci V, Milardi D, Campagna T, Gaglione M, Messere A, D'Urso A, Crisafi E, La Rosa C, Zarrelli A, Balzarini J, Di Fabio G
* Synthesis, biophysical characterization and anti-HIV activity of d(TG(3)AG) Quadruplexes bearing hydrophobic tails at the 5 '-end (365 views)
Bioorg Med Chem (ISSN: 0968-0896, 1464-3391, 0968-0896linking), 2014 Feb 1; 22(3): 960-966.
Impact Factor: 2.793
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Palmieri M, Malgieri G, Russo L, Baglivo I, Esposito S, Netti F, Del Gatto A, De Paola I, Zaccaro L, Pedone PV, Isernia C, Milardi D, Fattorusso R
* 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.
Impact Factor: 11.444
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Arena G, Fattorusso R, Grasso G, Grasso GI, Isernia C, Malgieri G, Milardi D, Rizzarelli E
* Zinc(II) complexes of ubiquitin: speciation, affinity and binding features (560 views)
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2011 Oct 4; 17(41): 11596-11603.
Impact Factor: 5.925
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Monfregola L, Bugatti V, Amodeo P, De Luca S, Vittoria V
* Physical and Water Sorption Properties of Chemically Modified Pectin with an Environmentally Friendly Process (286 views)
Biomacromolecules (ISSN: 1525-7797), 2011 Jun; 12(6): 2311-2318.
Impact Factor: 5.479
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Milardi D, Sciacca MFM, Pappalardo M, Grasso DM, La Rosa C
* The Role Of Aromatic Side-Chains In Amyloid Growth And Membrane Interaction Of The Islet Amyloid Polypeptide Fragment Lanflvh (458 views)
Eur Biophys J, 2011 Jan; 40(1): 1-12.
Impact Factor: 3.832
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Di Natale G, Pappalardo G, Milardi D, Sciacca MF, Attanasio F, La Mendola D, Rizzarelli E
* Membrane interactions and conformational preferences of human and avian prion N-terminal tandem repeats: The role of copper(II) ions, pH, and membrane mimicking environments (499 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2010 Nov 4; 114(43): 13830-13838.
Impact Factor: 3.603
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Sciacca MFM, Pappalardo M, Attanasio F, Milardi D, La Rosa C, Grasso DM
* Are fibril growth and membrane damage linked processes? An experimental and computational study of IAPP(12-18) and IAPP(21-27) peptides (402 views)
New J Chem (ISSN: 1144-0546), 2010; 34(2): 200-207.
Impact Factor: 2.631
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Sciacca MFM, Carbone V, Pappalardo M, Milardi D, La Rosa C, Grasso DM
* Interaction of human amylin with phosphatidylcholine and phosphatidylserine membranes (317 views)
Mol Cryst Liq Cryst (ISSN: 1542-1406), 2009; 500: 73-81.
Impact Factor: 0.451
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Sciacca MFM, Pappalardo M, Milardi D, Grasso DM, La Rosa C
* Calcium-Activated Membrane Interaction Of The Islet Amyloid Polypeptide: Implications In The Pathogenesis Of Type Ii Diabetes Mellitus (979 views)
Arch Biochem Biophys, 2008 Sep 15; 65(1-2): 291-298.
Impact Factor: 3.043
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De Pinto V, Tomasello F, Messina A, Guarino F, Benz R, La Mendola D, Magrì A, Milardi D, Pappalardo G
* Determination of the conformation of the human VDAC1 N-terminal peptide, a protein moiety essential for the functional properties of the pore (540 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2007 May 7; 8(7): 744-756.
Impact Factor: 3.446
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Pappalardo G, Milardi D, Magrì A, Attanasio F, Impellizzeri G, La Rosa C, Grasso D, Rizzarelli E
* Environmental factors differently affect human and rat IAPP: Conformational preferences and membrane interactions of IAPP17-29 peptide derivatives (655 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2007; 13(36): 10204-10215.
Impact Factor: 5.33
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Milardi D, Arnesano F, Grasso G, Magrì A, Tabbì G, Scintilla S, Natile G, Rizzarelli E
* Ubiquitin stability and the Lys63-linked polyubiquitination site are compromised on copper binding (378 views)
Angew Chem Int Ed (ISSN: 1433-7851, 1521-3773electronic, 1433-7851linking), 2007; 46(42): 7993-7995.
Impact Factor: 10.031
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Sciacca MFM, Milardi D, Pappalardo M, La Rosa C, Grasso DM
* Role of electrostatics in the thermal stability of ubiquitin: A combined DSC and MM study (248 views)
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2006 Nov; 86(2): 311-314.
Impact Factor: 1.438
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Bucci E, Vitagliano L, Barone R, Sorrentino S, D'Alessio G, Graziano G
* On the thermal stability of the two dimeric forms of ribonuclease (451 views)
Biophys Chem (ISSN: 0301-4622, 0301-4622linking), 2005 Jul 1; 116(2): 89-95.
Impact Factor: 1.925
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Pappalardo M, Milardi D, Grasso D, La Rosa C
* Phase behaviour of polymer-grafted DPPC membranes for drug delivery systems design (302 views)
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2005 May; 80(2): 413-418.
Impact Factor: 1.425
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La Rosa C, Milardi D, Amato E, Pappalardo M, Grasso D
* Molecular mechanism of the inhibition of cytochrome c aggregation by Phe-Gly (512 views)
Arch Bioch Bioph (ISSN: 0003-9861, 0003-9861linking), 2005 Mar 1; 435(1): 182-189.
Impact Factor: 3.152
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Grasso D, Milardi D, La Rosa C, Rizzarelli E
* The different role of Cu++ and Zn++ ions in affecting the interaction of prion peptide PrP106-126 with model membranes (298 views)
Chem Commun (ISSN: 1359-7345, 1364-548x, 1364-548xelectronic), 2004 Jan 21; 10(2): 246-247.
Impact Factor: 3.997
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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 (330 views)
Arch Bioch Bioph (ISSN: 0003-9861, 0003-9861linking), 2003 Jun 1; 414(1): 121-127.
Impact Factor: 2.338
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Guzzi R, Milardi D, La Rosa C, Grasso D, Verbeet MP, Canters GW, Sportelli L
* The effect of copper/zinc replacement on the folding free energy of wild type and Cys3Ala/Cys26Ala azurin (307 views)
Int J Biol Macromol (ISSN: 0141-8130, 0141-8130linking, 1879-0003electronic), 2003 Jan 15; 31(4-5): 163-170.
Impact Factor: 1.427
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Grasso D, Milardi D, Guantieri V, La Rosa C, Rizzarelli E
* Interaction of prion peptide PrP 180-193 with DPPC model membranes: A thermodynamic study (384 views)
New J Chem (ISSN: 1144-0546), 2003; 27(2): 359-364.
Impact Factor: 2.272
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Grasso D, Milardi D, La Rosa C, Impellizzeri G, Pappalardo G
* The interaction of a peptide with a scrambled hydrophobic/hydrophilic sequence (Pro-Asp-Ala-Asp-Ala-His-Ala-His-Ala-His-Ala-Ala-Ala-His-Gly) (PADH) with DPPC model membranes: A DSC study (276 views)
Thermochim Acta (ISSN: 0040-6031), 2002 Jul 15; 390(1-2): 73-78.
Impact Factor: 0.974
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Grasso D, Milardi D, La Rosa C, Rizzarelli E
* DSC study of the interaction of the prion peptide PrP106-126 with artificial membranes (378 views)
New J Chem (ISSN: 1144-0546), 2001; 25(12): 1543-1548.
Impact Factor: 2.44
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Martínez JC, Viguera AR, Berisio R, Wilmanns M, Mateo PL, Filimonov VV, Serrano L
Thermodynamic analysis of α-spectrin SH3 and two of its circular permutants with different loop lengths: Discerning the reasons for rapid folding in proteins (380 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 1999 Jan 12; 38(2): 549-559.
Impact Factor: 4.493
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28 Records (28 excluding Abstracts).
Total impact factor: 107.99 (107.99 excluding Abstracts).
Total 5 year impact factor: 117.722 (117.722 excluding Abstracts).
Total impact factor: 107.99 (107.99 excluding Abstracts).
Total 5 year impact factor: 117.722 (117.722 excluding Abstracts).
333 views. Last view on Saturday 27 May 2023, 3:06:33
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