Peptide mapping of bovine pancreatic ribonuclease A by reverse-phase high-performance liquid chromatography
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference17 articles.
1. Experimental studies of protein folding and unfolding
2. Multiple pathways for regenerating ribonuclease A
3. Intermediates in the refolding of reduced ribonuclease A
4. Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A.
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1. Chain reversals in model peptides: studies of cystine-containing cyclic peptides II. Effects of valyl residues and possible i-to-(i + 3) attractive ionic interactions on cyclization of [Cys1], [Cys6] hexapeptides;International Journal of Peptide and Protein Research;2009-01-12
2. Oxidative Folding of Leech-Derived Tryptase InhibitorViaNative Disulfide-Bonded Intermediates;Antioxidants & Redox Signaling;2008-01
3. Effects of column length, particle size, gradient length and flow rate on peak capacity of nano-scale liquid chromatography for peptide separations;Journal of Chromatography A;2007-04
4. Role of the [65−72] Disulfide Bond in Oxidative Folding of Bovine Pancreatic Ribonuclease A;Biochemistry;2003-09-10
5. Complete disulfide bond assignment of a recombinant immunoglobulin G4 monoclonal antibody;Analytical Biochemistry;2002-12
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