Mechanism of protein stabilization by disulfide bridges: calorimetric unfolding studies on disulfide-deficient mutants of the alpha-amylase inhibitor tendamistat.

@article{Vogl1995MechanismOP,
  title={Mechanism of protein stabilization by disulfide bridges: calorimetric unfolding studies on disulfide-deficient mutants of the alpha-amylase inhibitor tendamistat.},
  author={Thomas Vogl and R Brengelmann and H. J. Hinz and Matthias Scharf and M L{\"o}tzbeyer and Joachim W. Engels},
  journal={Journal of molecular biology},
  year={1995},
  volume={254 3},
  pages={481-96}
}
The present differential scanning calorimetry and circular dichroism studies on the mechanism of protein stabilization by disulfide bonds were concerned with two questions: is the increase in unfolding entropy upon removal of disulfide links sufficient for the explantation of the general stability decrease of disulfide-deficient mutants? Is it immaterial by which residue cysteine residues are replaced when disulfide bridges are to be opened? To answer these questions we investigated two… CONTINUE READING
9 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-9 of 9 extracted citations

Similar Papers

Loading similar papers…