Protein conformation and proton nuclear‐magnetic‐resonance chemical shifts Journal Article uri icon



  • The nuclear magnetic resonance (NMR) chemical shifts of the polypeptide backbone protons in basic pancreatic trypsin inhibitor from bovine organs and the inhibitors E and K from the venom of Dendroaspis polylepis polylepis have been analyzed. Using the corresponding shifts in model peptides, the chemical shifts observed in the proteins were decomposed into random‐coil shifts and conformation‐dependent shifts. Correlations between contributions to the latter term and the polypeptide conformation were investigated by using the crystal structure of the bovine inhibitor. In addition to the well‐known ring‐current effects, a correlation was found between chemical shifts of amide and Cα protons and the length of the hydrogen bonds formed by these protons with nearby oxygen atoms as acceptor groups. There remain sizeable and as yet unexplained residual conformation shifts. Overall, the present treatment provides a satisfactory qualitative explanation for the outstandingly large shifts of backbone hydrogen atoms in these diamagnetic proteins.

publication date

  • December 1, 1983

has restriction

  • bronze

Date in CU Experts

  • February 20, 2014 9:28 AM

Full Author List


author count

  • 3

Other Profiles

International Standard Serial Number (ISSN)

  • 0014-2956

Electronic International Standard Serial Number (EISSN)

  • 1432-1033

Additional Document Info

start page

  • 445

end page

  • 454


  • 137


  • 3