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. However, protein unfolding may cause an increase in the average distance between tyrosine and tryptophan residues, thus minimizing energy transfer and allowing detection of tyrosine emission
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. Only the 1g9f entry shows up the two proximal GIcNAc residues
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. As already mentioned above, the unfolding transition of proteins is not only characterized by the disappearance of the well-defined three-dimensional structure but can also cause distinct changes in the compactness of the unfolded structures or may induce pronounced protein aggregation
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. McLeish, University of Leeds, Physics and Astronomy, Woodhouse Lane, Leeds LS2 9JT, UK
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. The crossing-over of the complex and free buildup curves at ~6 ns (Fig
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. The solutions appeared visually clear for temperatures at or above 130°C and a dissolving time of 2 hours, but small nuclei below the visible range may still have remained
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. 1 is displayed in subsequent histograms
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