Sequential Melting of Two Hydrophobic Clusters Within The Green Fluorescent Protein Gfp-cycle3
Cluster Chemistry, Hydrophobicity, Imaging Probes, Melting, Protein Structure
Digital Object Identifier (DOI)
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.
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Citation / Publisher Attribution
Biochemistry, v. 50, issue 36, p. 7735-7744
Scholar Commons Citation
Melnik, Tatiana N.; Povarnitsyna, Tatiana V.; Glukhov, Anatoly S.; Uversky, Vladimir N.; and Melnik, Bogdan S., "Sequential Melting of Two Hydrophobic Clusters Within The Green Fluorescent Protein Gfp-cycle3" (2011). Molecular Medicine Faculty Publications. 485.