Nuclear magnetic resonance studies of linear, cyclic and polymeric peptides containing His, Ser and Asp residues spaced by ß alanylglycine
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3011.1986.tb01821.x/fullpdf
Reference22 articles.
1. Role of a Buried Acid Group in the Mechanism of Action of Chymotrypsin
2. Nitrogen-15 nuclear magnetic resonance spectroscopy. The state of histidine in the catalytic triad of .alpha.-lytic protease. Implications for the charge-relay mechanism of peptide-bond cleavage by serine proteases
3. Synthesis of linear, cyclic and polypeptides having the sequence -Asp-βAla-Gly-Ser-βAla-Gly-His-βAla-Gly- as catalysts in hydrolytic reactions
4. Catalytic activity of linear-, cyclic- and polypeptides having a sequence of -Asp-β-Ala-Gly-ser-β-Ala-Gly-His-β-Ala-Gly in the hydrolysis of p-nitrophenyl acetate
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1. Circular dichroism investigations on the conformation of linear, cyclic and polymeric peptides containing His, Ser and Asp residues;International Journal of Peptide and Protein Research;2009-01-12
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