作者: Ivana Sirangelo , Ettore Bismuto , Simona Tavassi , Gaetano Irace
DOI: 10.1016/S0167-4838(98)00038-7
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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 chromophores the aromatic residues, i.e., tyrosyl tryptophanyl extrinsic probe (8-anilino-1-naphthalenesulfonate, ANS) which is particularly useful for studying partly structured forms appearing in early stage of protein folding. emission decay as well resonance energy transfer from residues to ANS permitted identify characterize folded obtained under different experimental conditions. results indicate that so far detected (I-1 I-2 states) are distinct structural states. differences concern solvent accessibility side chains conformational dynamics region forming binding site fluorophore.