Journal article
Unfolding of apomyoglobin studied with two-dimensional correlations of tryptophan, 8-anilino-1-naphthalenesulfonate, and pyrene fluorescence
Journal of molecular structure, Vol.799(1), pp.177-187
2006
DOI: 10.1016/j.molstruc.2006.04.007
Abstract
Acid-induced unfolding of horse apomyoglobin is studied with fluorescence of tryptophan residues and extrinsic probes 8-anilino-1-naphthalenesulfonate (ANS) and pyrene. Two-dimensional statistical correlation coefficient analysis of tryptophan, ANS and pyrene fluorescence reveals that apomyoglobin unfolds in two steps via a folding intermediate. Both tryptophan and ANS fluorescence show microenvironment-sensitive emission maximum and fluorescence intensity. Hetero-spectral 2D correlation analysis reveals that the “red” tryptophan fluorescence correlates with the “red” ANS fluorescence, and the “blue” correlates with the “blue” in the acid-induced unfolding process. Correlation curves are established between the hydrophobicity of the probe-binding site(s) as disclosed by ANS and pyrene fluorescence and the folding extent of apomyoglobin as indicated by tryptophan fluorescence. Two anion-induced refolding intermediates of apomyoglobin: Cl
−-induced A-1, and trichloroacetate (TCA)-induced I-2 do not follow the correlation trajectory in the acid-induced unfolding. This suggests that the two anion-induced intermediates do not belong to the low-salt acid-unfolding pathway of apomyoglobin.
Details
- Title: Subtitle
- Unfolding of apomyoglobin studied with two-dimensional correlations of tryptophan, 8-anilino-1-naphthalenesulfonate, and pyrene fluorescence
- Creators
- Gufeng WangM. Lei Geng
- Resource Type
- Journal article
- Publication Details
- Journal of molecular structure, Vol.799(1), pp.177-187
- Publisher
- Elsevier B.V
- DOI
- 10.1016/j.molstruc.2006.04.007
- ISSN
- 0022-2860
- eISSN
- 1872-8014
- Language
- English
- Date published
- 2006
- Academic Unit
- Chemistry
- Record Identifier
- 9984216681202771
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