Literature DB >> 11368526

Copper stabilizes azurin by decreasing the unfolding rate.

I Pozdnyakova1, J Guidry, P Wittung-Stafshede.   

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Year:  2001        PMID: 11368526     DOI: 10.1006/abbi.2000.2369

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN: 0003-9861            Impact factor:   4.013


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  12 in total

1.  Studies of Pseudomonas aeruginosa azurin mutants: cavities in beta-barrel do not affect refolding speed.

Authors:  Irina Pozdnyakova; Jesse Guidry; Pernilla Wittung-Stafshede
Journal:  Biophys J       Date:  2002-05       Impact factor: 4.033

2.  Role of structural determinants in folding of the sandwich-like protein Pseudomonas aeruginosa azurin.

Authors:  Corey J Wilson; Pernilla Wittung-Stafshede
Journal:  Proc Natl Acad Sci U S A       Date:  2005-03-07       Impact factor: 11.205

3.  Quantification of excluded volume effects on the folding landscape of Pseudomonas aeruginosa apoazurin in vitro.

Authors:  Alexander Christiansen; Pernilla Wittung-Stafshede
Journal:  Biophys J       Date:  2013-10-01       Impact factor: 4.033

4.  Cavity-creating mutations in Pseudomonas aeruginosa azurin: effects on protein dynamics and stability.

Authors:  Edi Gabellieri; Ettore Balestreri; Alvaro Galli; Patrizia Cioni
Journal:  Biophys J       Date:  2008-04-18       Impact factor: 4.033

5.  Changes in non-core regions stabilise plastocyanin from the thermophilic cyanobacterium Phormidium laminosum.

Authors:  Francisco J Muñoz-López; Simone Raugei; Miguel A De la Rosa; Antonio J Díaz-Quintana; Paolo Carloni
Journal:  J Biol Inorg Chem       Date:  2010-03       Impact factor: 3.358

6.  Stabilization of protein structure through π-π interaction in the second coordination sphere of pseudoazurin.

Authors:  Takahide Yamaguchi; Yuko Nihei; Duncan E K Sutherland; Martin J Stillman; Takamitsu Kohzuma
Journal:  Protein Sci       Date:  2017-07-20       Impact factor: 6.725

7.  The removal of a disulfide bridge in CotA-laccase changes the slower motion dynamics involved in copper binding but has no effect on the thermodynamic stability.

Authors:  André T Fernandes; Manuela M Pereira; Catarina S Silva; Peter F Lindley; Isabel Bento; Eduardo Pinho Melo; Lígia O Martins
Journal:  J Biol Inorg Chem       Date:  2011-03-03       Impact factor: 3.358

8.  Apo-azurin folds via an intermediate that resembles the molten-globule.

Authors:  Anders Sandberg; Johan Leckner; B Göran Karlsson
Journal:  Protein Sci       Date:  2004-10       Impact factor: 6.725

9.  Conformational changes in azurin from Pseudomona aeruginosa induced through chemical and physical protocols.

Authors:  Lymari Fuentes; Jessica Oyola; Mónica Fernández; Edwin Quiñones
Journal:  Biophys J       Date:  2004-09       Impact factor: 4.033

10.  Role of copper in thermal stability of human ceruloplasmin.

Authors:  Erik Sedlák; Gabriel Zoldák; Pernilla Wittung-Stafshede
Journal:  Biophys J       Date:  2007-10-26       Impact factor: 4.033

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