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. The observations that so many eukaryotic proteins are glycosylated and that N-linked glycosylation is more frequently observed in proteins suggest that N-linked glycans are a prime requisite for sustaining the structure-function equilibrium in many proteins (6)
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. Even for TAKA, which does not show any aggregation, we observed slightly smaller red shift for thermal unfolding, but due to missing aggregation still larger as compared to BLA, BAA, and BSUA
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. The fluorescence intensity of Bis-ANS decreases as the A-state aggregates, well in accordance with hiding of accessible surface area in contrast to the behavior of ANS, likely due to the fact that Bis-ANS is more bulky
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. RESULTS AND DISCUSSIONPrefibrillar stageFig
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. The true number is probably larger because on average protein sites exhibit ANS fluorescence yields much lower than 0
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.5-ns internal motion in the CaM:SEF2-1mp complex can be attributed to motions of the separate N- and C-terminal domains of CaM, because the free domains have an overall correlation time of ~3 ns
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