Datta, Deepshikha and Mayo, Stephen L. (2002) A designed apoplastocyanin variant that shows reversible folding. Biochemical and Biophysical Research Communications, 296 (4). pp. 988-990. ISSN 0006-291X. http://resolver.caltech.edu/CaltechAUTHORS:20110620-160423337
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Plastocyanin, like many other metalloproteins, does not undergo reversible folding, which is thought to be due to an irreversible conformational change in the copper-binding site. Moreover, apoplastocyanin's ability to adopt a native tertiary structure is highly salt-dependent, and even in high salt, it has an irreversible thermal denaturation. Here, we report a designed apoplastocyanin variant, PCV, that is well folded and has reversible folding in both high and low salt conditions. This variant provides a tractable model for understanding and designing protein β-sheets.
|Additional Information:||© 2002 Elsevier Science. Received 31 July 2002; Available online 21 August 2002.|
|Subject Keywords:||Temperature; Copper; Circular Dichroism; Escherichia coli; Apoproteins; Plant Proteins; Crystallography: X-Ray; Plastocyanin; Salts; Protein Folding; Mutagenesis: Site-Directed; Protein Conformation; Protein Structure: Secondary; Binding Sites; Protein Structure: Tertiary; Plastocyanin; Reversible folding; Copper-binding site; Protein design|
|Official Citation:||Deepshikha Datta, Stephen L Mayo, A designed apoplastocyanin variant that shows reversible folding, Biochemical and Biophysical Research Communications, Volume 296, Issue 4, 30 August 2002, Pages 988-990, ISSN 0006-291X, 10.1016/S0006-291X(02)02037-5.|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Marie Ary|
|Deposited On:||03 Oct 2011 22:46|
|Last Modified:||23 Aug 2016 10:02|
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