"Sequential Melting of Two Hydrophobic Clusters Within The Green Fluore" by Tatiana N. Melnik, Tatiana V. Povarnitsyna et al.
 

Sequential Melting of Two Hydrophobic Clusters Within The Green Fluorescent Protein Gfp-cycle3

Document Type

Article

Publication Date

2011

Keywords

Cluster Chemistry, Hydrophobicity, Imaging Probes, Melting, Protein Structure

Digital Object Identifier (DOI)

https://doi.org/10.1021/bi2006674

Abstract

The analysis of the three-dimensional structure of green fluorescent protein (GFP-cycle3) revealed the presence of two well-defined hydrophobic clusters located on the opposite sides of the GFP β-can that might contribute to the formation of partially folded intermediate(s) during GFP unfolding. The microcalorimetric analysis of the nonequilibrium melting of GFP-cycle3 and its two mutants, I14A and I161A, revealed that due to the sequential melting of the mentioned hydrophobic clusters, the temperature-induced denaturation of this protein most likely occurs in three stages. The first and second stages involve melting of a smaller hydrophobic cluster formed around the residue I161, whereas a larger hydrophobic cluster (formed around the residues I14) is melted only at the last GFP-cycle3 denaturation step or remains rather structured even in the denatured state.

Was this content written or created while at USF?

Yes

Citation / Publisher Attribution

Biochemistry, v. 50, issue 36, p. 7735-7744

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