Hydrogen-bonded structure and 13C NMR chemical shift tensor of amino acid residue carbonyl carbons of peptides and polypeptides in the crystalline state. Part I-Reference-Cited by-同舟云学术

Hydrogen-bonded structure and 13C NMR chemical shift tensor of amino acid residue carbonyl carbons of peptides and polypeptides in the crystalline state. Part I

Published:1996-10 Issue:1 Volume:384 Page:17-23
ISSN:0022-2860
Container-title:Journal of Molecular Structure
language:en
Short-container-title:Journal of Molecular Structure

Author:

Kameda T.,Takeda N.,Kuroki S.,Kurosu H.,Ando S.,Ando I.,Shoji A.,Ozaki T.

Publisher

Elsevier BV

Subject

Inorganic Chemistry,Organic Chemistry,Spectroscopy,Analytical Chemistry

Reference34 articles.

1. Conformation in Fibrous Proteins;Fraser,1973

2. Spectroscopic Studies of the Hydrogen Bond

3. Infrared spectra of strongly hydrogen-bonded systems

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

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

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