Characterization of low populated peptide helical structures in solution by means of NMR proton conformational shifts
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference20 articles.
1. Seeding protein folding
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4. Nuclear Overhauser effects in aqueous solution as dynamic probes in short linear peptides
5. Folding of a peptide corresponding to the .alpha.-helix in bovine pancreatic trypsin inhibitor
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