A study of hydrogen-bonding of amino acids, peptides and polypeptides in the solid state as a function of temperature by static 2H NMR method
Author:
Publisher
Elsevier BV
Subject
Inorganic Chemistry,Organic Chemistry,Spectroscopy,Analytical Chemistry
Reference52 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. Hydrogen-bonding effect on 13C NMR chemical shifts of amino acid residue carbonyl carbons of some peptides in the crystalline state
4. 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
5. The relationship between the helical conformation and 13C NMR chemical shift of amino acid residue carbonyl carbons of polypeptides in the solid state
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