ArticleProceedings of the National Academy of Sciences of the United States of America2005
Role of structural determinants in folding of the sandwich-like protein Pseudomonas aeruginosa azurin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Mutational Analysis of Protein Folding Transition States: Phi Values.Methods in molecular biology (Clifton, N.J.) · 2022Article
- A Euclidean perspective on the unfolding of azurin: chain motion.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- The sole tryptophan of amicyanin enhances its thermal stability but does not influence the electronic properties of the type 1 copper site.Archives of biochemistry and biophysics · 2014Article
- Quantification of excluded volume effects on the folding landscape of Pseudomonas aeruginosa apoazurin in vitro.Biophysical journal · 2013Article
- Dynamics and unfolding pathway of chimeric azurin variants: insights from molecular dynamics simulation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
- A Euclidean Perspective on the Unfolding of Azurin: Spatial Correlations.Molecular physics · 2013Article
- Investigation of an anomalously accelerating substitution in the folding of a prototypical two-state protein.Journal of molecular biology · 2010Article
- Practical approaches to protein folding and assembly: spectroscopic strategies in thermodynamics and kinetics.Methods in enzymology · 2009Article
- In vitro unfolding of yeast multicopper oxidase Fet3p variants reveals unique role of each metal site.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Cavity-creating mutations in Pseudomonas aeruginosa azurin: effects on protein dynamics and stability.Biophysical journal · 2008Article
- Minimizing frustration by folding in an aqueous environment.Archives of biochemistry and biophysics · 2008Article
- Establishing the entatic state in folding metallated Pseudomonas aeruginosa azurin.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Solvation of the folding-transition state in Pseudomonas aeruginosa azurin is modulated by metal: Solvation of azurin's folding nucleus.Protein science : a publication of the Protein Society · 2006Article
- Strict rules determine arrangements of strands in sandwich proteins.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- A geometric construction determines all permissible strand arrangements of sandwich proteins.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
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2 authors.
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Abstract
An invariant substructure that forms two interlocked pairs of neighboring beta-strands occurs in essentially all known sandwich-like proteins. Eight conserved positions in these strands were recently shown to act as structural determinants. To test whether the residues at these invariant positions are conserved for mechanistic (i.e., part of folding nucleus) or energetic (i.e., governing native-state stability) reasons, we characterized the folding behavior of eight point-mutated variants of the sandwich-like protein Pseudomonas aeruginosa apo-azurin. We find a simple relationship among the conserved positions: half of the residues form native-like interactions in the folding transition state, whereas the others do not participate in the folding nucleus but govern high native-state stability. Thus, evolutionary preservation of these specific positions gives both mechanistic and energetic advantages to members of the sandwich-like protein family.
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