Thermodynamics Of Azurin Folding: The Role Of The Copper Ion (716 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:
Not available.
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:
Not available.
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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View Export to BibTeX Export to EndNote
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Impact Factor: 10.031
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View Export to BibTeX Export to EndNote
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Impact Factor: 2.338
View Export to BibTeX Export to EndNote
Guzzi R, Milardi D, La Rosa C, Grasso D, Verbeet MP, Canters GW, Sportelli L
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Impact Factor: 1.427
View Export to BibTeX Export to EndNote
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Impact Factor: 2.272
View Export to BibTeX Export to EndNote
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 (684 views)
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Impact Factor: 0.974
View Export to BibTeX Export to EndNote
Grasso D, Milardi D, La Rosa C, Rizzarelli E
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New J Chem (ISSN: 1144-0546), 2001; 25(12): 1543-1548.
Impact Factor: 2.44
View Export to BibTeX Export to EndNote
Martínez JC, Viguera AR, Berisio R, Wilmanns M, Mateo PL, Filimonov VV, Serrano L
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Impact Factor: 4.493
View Export to BibTeX Export to EndNote
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).
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