Investigation of folding in protamine by FTIR.

@article{Pesek1992InvestigationOF,
  title={Investigation of folding in protamine by FTIR.},
  author={Joseph J Pesek and F R Shabary},
  journal={Talanta},
  year={1992},
  volume={39 10},
  pages={
          1215-8
        }
}
The secondary structure of purified protamine, a non-specific DNA binding protein, was studied in solution at pH 4, 7 and 8 by FTIR. This permitted analysis of the folded form of the protein (acidic pH) as well as the folded conformers (neutral and basic pH). Hg(2+) was utilized to probe the accessibility of the free thiol groups (cysteine residues). The SH groups form when disulfides, which play the major role in stabilizing the conformation of this protein, are broken. It was possible to… CONTINUE READING
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