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. The IR and fluorescence results strongly suggested that the thermal unfolding of ACYI could be illustrated as a two-stage process involving an intermediate: native state (N) [arrow right] intermediate stale (I) [arrow right] aggregates (A)
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. In either case the conclusion is that in the frozen state the polypeptide structure of the putative binding sites has changed, becoming unable to host ANS or to enhance its fluorescence yield, as when the probe surrounding changes from rigid to mobile (26)
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. Upon Ca^sup 2+^ binding, a conformational change enables it to interact with over 100 different target proteins, including transcription factors (for reviews, see Van Eldik and Watterson and others (6,7))
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. The importance of diffusive searches is unsurprising, since under biological conditions, all candidates for energetic interactions, including electrostatics, are locally screened to a few angstroms: much smaller than the dimensions over which sections of protein must move to find their native configurations
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. Manuscript submitted 4 April 2003 to Scientific Editor's Office
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