Terbium luminescence-lifetime heterogeneity and protein equilibrium conformational dynamics.

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.

authors

Austin RH,Stein DL,Wang J

doi

10.1073/pnas.84.6.1541

subject

Has Abstract

pub_date

1987-03-01 00:00:00

pages

1541-5

issue

6

eissn

0027-8424

issn

1091-6490

journal_volume

84

pub_type

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