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Biochemistry. 2011 Sep 13;50(36):7735-44. doi: 10.1021/bi2006674. Epub 2011 Aug 17.

Sequential melting of two hydrophobic clusters within the green fluorescent protein GFP-cycle3.

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Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.


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.

[Indexed for MEDLINE]

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