Kinetic studies on the unfolding and refolding of pepsinogen in urea. The nature of the rate-limiting step.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference24 articles.
1. Native and Unfolded States of Pepsinogen
2. Thermodynamics of the denaturation of pepsinogen by urea
3. Experimental studies of protein folding and unfolding
4. Native and Unfolded States of Pepsinogen
5. The alkaline transition of swine pepsinogen
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2. Protein quality control in the ER: The recognition of misfolded proteins;Seminars in Cell & Developmental Biology;2010-07
3. An investigation of the thermal unfolding of swine pepsinogen using circular dichroism;Archives of Biochemistry and Biophysics;1992-02
4. A reversible unfolding reaction of swine pepsin; implications for pepsinogen's folding mechanism;Biochemical and Biophysical Research Communications;1989-01
5. Proline isomerization and the slow folding reactions of the α subunit of tryptophan synthase from Escherichia coli;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1987-06
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