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. 1987 Mar;84(6):1541–1545. doi: 10.1073/pnas.84.6.1541

Terbium luminescence-lifetime heterogeneity and protein equilibrium conformational dynamics.

R H Austin, D L Stein, J Wang
PMCID: PMC304471  PMID: 3470740

Abstract

The fluorescence decay of the rare earth terbium when bound to the protein calmodulin changes from a simple exponential decay to a complex nonexponential decay as the temperature is lowered below 200 K. We have fit the observed decay curves by assuming that the terbium emission is a forced electric dipole transition and proteins have a distribution of continuous conformational states. Quantitative fits to the data indicate that the root-mean-square configurational deviation of the atoms surrounding the terbium ion is 0.2 A, in good agreement with other measurements. We further point out that because the protein seems to undergo a glass transition yet retains configurational order at room temperature, the proper name for the physical state of a protein at room temperature is the rubber-like state.

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Selected References

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