Effects of urea and guanidine · HCl on the folding and unfolding of pancreatic trypsin inhibitor
- 1 June 1977
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 113 (2) , 313-328
- https://doi.org/10.1016/0022-2836(77)90144-9
Abstract
No abstract availableThis publication has 17 references indexed in Scilit:
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- The single-disulphide intermediates in the refolding of reduced pancreatic trypsin inhibitorJournal of Molecular Biology, 1974
- Intermediates in the refolding of reduced pancreatic trypsin inhibitorJournal of Molecular Biology, 1974
- Renaturation of the reduced bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1974
- Proton magnetic resonance investigation of the conformational properties of the basic pancreatic trypsin inhibitorFEBS Letters, 1973
- Extended conformations of polypeptides and proteins in urea and guanidine hydrochlorideBiopolymers, 1973
- The Conformational Properties of the Basic Pancreatic Trypsin-InhibitorEuropean Journal of Biochemistry, 1971