Native and Unfolded States of Pepsinogen
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference21 articles.
1. The Amino Acid Composition of Chromatographically Purified Pepsinogen
2. The optical rotatory properties of pepsinogen
3. Pepsinogen and Pepsin
4. KINETICS OF THE FORMATION OF PEPSIN FROM SWINE PEPSINOGEN AND IDENTIFICATION OF AN INTERMEDIATE COMPOUND
5. Dependence of the optical-rotatory properties of pepsinogen on solvent and temperature
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1. Recombinant prosegment peptide acts as a folding catalyst and inhibitor of native pepsin;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2009-12
2. Comparison of Solution Structures and Stabilities of Native, Partially Unfolded and Partially Refolded Pepsin;Biochemistry;2006-11-01
3. The origin of the intermediates detected in the folding of swine pepsinogen.;Journal of Biological Chemistry;1982-01
4. Comparative thermodynamic study of pepsinogen and pepsin structure;Journal of Molecular Biology;1981-10
5. Kinetic studies on the unfolding and refolding of pepsinogen in urea. The nature of the rate-limiting step.;Journal of Biological Chemistry;1980-05
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