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March 1, 1961Journal of the American Chemical Society

The Properties of Thyroglobulin. VI. The Internal Rigidity of Native and Denatured Thyroglobulin

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Authors

RSRobert F. SteinerUniversity of Maryland, BaltimoreHEHarold EdelhochNational Institutes of Health

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Overview

Experimental study demonstrates reversible loss of internal rigidity during thyroglobulin denaturation, indicating fluorescence polarization tracks protein structural disorganization.

Key Points

  • To determine the rotational relaxation time and internal structural rigidity of native thyroglobulin compared to its denatured states.
  • Coupled a fluorescent dye to thyroglobulin and evaluated rotational relaxation time using fluorescence polarization measurements.
  • Treated the protein with denaturing agents, including urea, guanidine, detergent, and alkali, with or without sulfhydryl reagents, followed by dilution recovery assays.
  • Correlated polarization changes with hydrodynamic measurements of protein conformational modifications.
  • Detergent and urea treatments markedly decreased the rotational relaxation time of thyroglobulin, which was fully restored upon dilution.
  • Sulfhydryl reagents further decreased relaxation times only in detergent-treated samples, and alkaline exposure produced a time-dependent polarization drop in the presence of 8M urea or 5M guanidine.
  • Changes in fluorescence polarization aligned with hydrodynamic conformational assays, confirming the utility of polarization for assessing internal protein disorganization.

Cite This Study

Steiner et al. (1961) studied this question.

synapsesocial.com/papers/6a902a60f5c79ce9992da04dhttps://doi.org/10.1021/ja01467a040
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