Hydrogen-bonding effect on 13C NMR chemical shifts of amino acid residue carbonyl carbons of some peptides in the crystalline state-Reference-Cited by-同舟云学术

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Hydrogen-bonding effect on 13C NMR chemical shifts of amino acid residue carbonyl carbons of some peptides in the crystalline state

Published:1995-05 Issue:3 Volume:350 Page:233-240
ISSN:0022-2860
Container-title:Journal of Molecular Structure
language:en
Short-container-title:Journal of Molecular Structure

Author:

Tsuchiya Kaoru,Takahashi Akihiro,Takeda Naoto,Asakawa Naoki,Kuroki Shigeki,Ando Isao,Shoji Akira,Ozaki Takuo

Publisher

Elsevier BV

Subject

Inorganic Chemistry,Organic Chemistry,Spectroscopy,Analytical Chemistry

Reference41 articles.

1. Intermolecular hydrogen-bonding effect on carbon-13 NMR chemical shifts of glycine residue carbonyl carbons of peptides in the solid state

2. Hydrogen-bonding effect on carbon-13 NMR chemical shifts of L-alanine residue carbonyl carbons of peptides in the solid state

3. Conformation-dependent carbon-13 NMR chemical shifts of poly(L-alanine) in the solid state: FPT INDO calculation of N-acetyl-N'-methyl-L-alanine amide as a model compound of poly(L-alanine)

4. Theory of NMR Parameters;Ando,1983

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