Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: Synergism among multiple depletions (454 views)
Arch Bioch Bioph (ISSN: 0003-9861, 0003-9861linking), 2003 Jun 1; 414(1): 121-127.
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Paper type: Journal Article,
Impact factor: 2.338, 5-year impact factor: 3.252
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0038706158&partnerID=40&md5=661f0677e3ad0293e3a54a1f582eead9
Keywords: Azurin, Copper, Differential Scanning Calorimetry, Disulfide Bridge, Stability, Apo Azurin, Apo Azurin C26 A, Apo Azurin C3 A, Apolipoprotein, Apolipoprotein C26 A, Apolipoprotein C3 A, Copper Ion, Copper Protein, Cysteine, Holo Azurin, Holo Azurin C26 A, Holo Azurin C3 A, Mutant Protein, Unclassified Drug, Amino Acid Substitution, Article, Comparative Study, Depletion, Parameter, Priority Journal, Protein Folding, Protein Stability, Temperature, Thermodynamics, Energy Transfer, Escherichia Coli, Models, Chemical, Mutagenesis, Site-Directed, Protein Conformation, Protein Denaturation, Protein Engineering,
Affiliations:
*** IBB - CNR ***
Ist. Biostrutture e Bioimmagini-CNR, Sezione di Catania, Viale Andrea Doria 6, 95125 Catania, Italy
Dipartimento di Scienze Chimiche, Universita' di Catania, Viale Andrea Doria 6, 95125 Catania, Italy
Gorleaus Laboratories, Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA Leiden, Netherlands
References:
Not available.
Arch Bioch Bioph (ISSN: 0003-9861, 0003-9861linking), 2003 Jun 1; 414(1): 121-127.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.338, 5-year impact factor: 3.252
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0038706158&partnerID=40&md5=661f0677e3ad0293e3a54a1f582eead9
Keywords: Azurin, Copper, Differential Scanning Calorimetry, Disulfide Bridge, Stability, Apo Azurin, Apo Azurin C26 A, Apo Azurin C3 A, Apolipoprotein, Apolipoprotein C26 A, Apolipoprotein C3 A, Copper Ion, Copper Protein, Cysteine, Holo Azurin, Holo Azurin C26 A, Holo Azurin C3 A, Mutant Protein, Unclassified Drug, Amino Acid Substitution, Article, Comparative Study, Depletion, Parameter, Priority Journal, Protein Folding, Protein Stability, Temperature, Thermodynamics, Energy Transfer, Escherichia Coli, Models, Chemical, Mutagenesis, Site-Directed, Protein Conformation, Protein Denaturation, Protein Engineering,
Affiliations:
*** IBB - CNR ***
Ist. Biostrutture e Bioimmagini-CNR, Sezione di Catania, Viale Andrea Doria 6, 95125 Catania, Italy
Dipartimento di Scienze Chimiche, Universita' di Catania, Viale Andrea Doria 6, 95125 Catania, Italy
Gorleaus Laboratories, Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA Leiden, Netherlands
References:
Not available.
Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: Synergism among multiple depletions
The stabilizing potential of the copper ion and the disulfide bridge in azurin has been explored with the aim of inspecting the ways in which these two factors influence one another. Specifically, whether copper and disulfide contributions to protein stability are additive has been examined. To this aim, the thermal unfolding of a copper-depleted mutant lacking the disulfide bridge between Cys3 and Cys26 (apo C3A/C26A azurin) was studied by differential scanning calorimetry. A comparison of the unfolding parameters of holo and apo C3A/C26A azurin with the apo C3A/C26A protein has shown that the effects of simultaneous copper and disulfide depletion are additive only at two temperatures: T=15°C and T=67°C. Within this range the presence of the copper ion and the disulfide bridge has a positive synergistic effect on azurin stability. These findings might have implications for the rational use of the stabilizing potential of copper and disulfides in copper protein engineering. © 2003 Elsevier Science (USA). All rights reserved.
The stabilizing potential of the copper ion and the disulfide bridge in azurin has been explored with the aim of inspecting the ways in which these two factors influence one another. Specifically, whether copper and disulfide contributions to protein stability are additive has been examined. To this aim, the thermal unfolding of a copper-depleted mutant lacking the disulfide bridge between Cys3 and Cys26 (apo C3A/C26A azurin) was studied by differential scanning calorimetry. A comparison of the unfolding parameters of holo and apo C3A/C26A azurin with the apo C3A/C26A protein has shown that the effects of simultaneous copper and disulfide depletion are additive only at two temperatures: T=15°C and T=67°C. Within this range the presence of the copper ion and the disulfide bridge has a positive synergistic effect on azurin stability. These findings might have implications for the rational use of the stabilizing potential of copper and disulfides in copper protein engineering. © 2003 Elsevier Science (USA). All rights reserved.
Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: Synergism among multiple depletions
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Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: Synergism among multiple depletions
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Milardi D, Pappalardo M, Pannuzzo M, Grasso DM, Rosa CL
* The role of the Cys2-Cys7 disulfide bridge in the early steps of Islet amyloid polypeptide aggregation: A molecular dynamics study (489 views)
Chem Phys Lett (ISSN: 0009-2614), 2008 Oct 1; 463(4-6): 396-399.
Impact Factor: 2.169
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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 (1167 views)
Arch Biochem Biophys, 2008 Sep 15; 65(1-2): 291-298.
Impact Factor: 3.043
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Pappalardo M, Sciacca MFM, Milardi D, Grasso DM, La Rosa C
* Thermodynamics Of Azurin Folding: The Role Of The Copper Ion (409 views)
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2008 Sep; 93(2): 575-581.
Impact Factor: 1.63
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Dalla Serra M, Cirioni O, Vitale RM, Renzone G, Coraiola M, Giacometti A, Potrich C, Baroni E, Guella G, Sanseverino M, De Luca S, Scalise G, Amodeo P, Scaloni A
* Structural features of distinctin affecting peptide biological and biochemical properties (782 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2008 Jul 29; 47(30): 7888-7899.
Impact Factor: 3.379
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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 (731 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 (782 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 (481 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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De Simone A, Berisio R, Zagari A, Vitagliano L
* Limited Tendency Of Alpha-Helical Residues To Form Disulfide Bridges: A Structural Explanation (602 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 740-747.
Impact Factor: 1.801
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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 (334 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 (608 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 (344 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 (668 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 (372 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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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 (402 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 (568 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 (417 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 (414 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 (1064 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 1999 Jan 12; 38(2): 549-559.
Impact Factor: 4.493
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36 Records (36 excluding Abstracts).
Total impact factor: 132.572 (132.572 excluding Abstracts).
Total 5 year impact factor: 139.831 (139.831 excluding Abstracts).
Total impact factor: 132.572 (132.572 excluding Abstracts).
Total 5 year impact factor: 139.831 (139.831 excluding Abstracts).
454 views. Last view on Saturday 12 October 2024, 4:17:16
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