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首页> 外文期刊>Biochimica et Biophysica Acta. Protein Structure and Molecular Enzymology >Apomyoglobin folding intermediates characterized by the hydrophobic fluorescent probe 8-anilino-1-naphthalene sulfonate (ANS)
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Apomyoglobin folding intermediates characterized by the hydrophobic fluorescent probe 8-anilino-1-naphthalene sulfonate (ANS)

机译：肌红蛋白折叠中间体，其特征在于疏水荧光探针8-苯胺基-1-萘磺酸盐（ANS）

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摘要

Folding apomyoglobin intermediates were investigated by optical techniques including steady-state fluorescence, frequency domain fluorometry, and absorption spectroscopy. The investigated chromophores were the aromatic residues, i.e., tyrosyl and tryptophanyl residues, and the extrinsic probe (8-anilino-1-naphthalenesulfonate, ANS) which is particularly useful or studying partly structured forms appearing in the early stage of protein folding. The emission decay of the extrinsic probe as well as resonance energy transfer from tryptophanyl residues to ANS permitted to identify and characterize partly folded forms obtained under different experimental conditions. The results indicate that the intermediates so far detected (I-1 and I-2 states) are distinct structural states. The differences concern the solvent accessibility to the aromatic side chains and the conformational dynamics of the protein region forming the binding site for the extrinsic fluorophore.
机译：通过包括稳态荧光，频域荧光法和吸收光谱法在内的光学技术研究折叠的肌红蛋白中间体。所研究的发色团是芳香族残基，即酪氨酰基和色氨酸残基，以及非本征探针（8-苯胺基-1-萘磺酸盐，ANS），它特别有用或研究蛋白质折叠早期出现的部分结构化形式。外在探针的发射衰减以及从色氨酸残基到ANS的共振能量转移，可以鉴定和表征在不同实验条件下获得的部分折叠形式。结果表明，到目前为止检测到的中间体（I-1和I-2状态）是不同的结构状态。差异涉及芳族侧链的溶剂可及性和形成外源荧光团结合位点的蛋白质区域的构象动力学。

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