1H NMR titration shifts of amide proton resonances in polypeptide chains
暂无分享，去创建一个
[1] A. Go,et al. Studies of peptide conformation: Backbone folding of tetrapeptide derivatives in methanol and water , 1976, Biopolymers.
[2] Y. Rahamim,et al. Nmr studies of aqueous solutions of tetra and branched peptides. I. Sequence determination of amino‐acid residues and the assignment of peptide hydrogen signals , 1976, Biopolymers.
[3] M. Llinás,et al. Solution conformation of the ferrichromes. VI. Charge relay at the peptide bond. Proton magnetic resonance study of solvation effects on the amide electron density distribution , 1975 .
[4] K. Wüthrich,et al. Carbon-13 NNIR of the protected tetrapeptides TFA-Gly-Gly-L-X-L-Ala-OCH3, where X stands for the 20 common amino acids , 1974 .
[5] K. Wüthrich,et al. Proton magnetic resonance investigation of the conformational properties of the basic pancreatic trypsin inhibitor , 1973, FEBS letters.
[6] B. Sykes,et al. A nuclear magnetic resonance study of bovine pancreatic trypsin inhibitor. Tyrosine titrations and backbone NH groups. , 1973, Biochemistry.
[7] G. Némethy,et al. The γ Turn, a Possible Folded Conformation of the Polypeptide Chain. Comparison with the β Turn , 1972 .
[8] D. Urry,et al. Temperature dependence of amide proton chemical shifts: the secondary structures of gramicidin S and valinomycin. , 1969, Biochemical and biophysical research communications.