Transient conformational states in proteins followed by differential labeling.

  • C Ghélis
  • Published 1980 in Biophysical journal

Abstract

Refolding of previously denatured and reduced elastase has been followed by titration of chemical reactivities of amino acid side chains to study the topography of the protein in the native state, and the microenvironment variations of protein side chains during the structural transition. Groups accessible to chemical reagents in the denatured form and… (More)

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Cite this paper

@article{Ghlis1980TransientCS, title={Transient conformational states in proteins followed by differential labeling.}, author={C Gh{\'e}lis}, journal={Biophysical journal}, year={1980}, volume={32 1}, pages={503-14} }