Macrocyclic Enzyme Model Systems. Catalytic Activity of Cyclic Peptides Involving Hydrophobic Segments
Author:
Publisher
The Chemical Society of Japan
Subject
General Chemistry
Link
https://www.jstage.jst.go.jp/article/bcsj1926/51/9/51_9_2690/_pdf
Reference25 articles.
1. "Artificial enzyme" combining a metal catalytic group and a hydrophobic binding cavity
2. A Macrocyclic Enzyme Model System. Acyl Transfer fromp-Nitrophenyl Carboxylates to Paracyclophane Oxime
3. A Macrocyclic Enzyme Model System. Substrate Specificity for the Inclusion into Paracyclophane Oxime and the Subsequent Acyl Transfer Reaction
4. A Macrocyclic Enzyme Model System. An Electrostatic-Hydrophobic Double-Field Catalysis by a [20]Paracyclophane in the Deacylation ofp-Nitrophenyl Hexadecanoate
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1. Synthesis, conformation and reactivity towards p-nitrophenyl acetate of polypeptides incorporating aspartic acid, serine and histidine;International Journal of Peptide and Protein Research;2009-01-12
2. Hydrolysis of various types of ester substrates with linear, cyclic and polymeric peptides containing His, Ser and Asp residues;International Journal of Peptide and Protein Research;2009-01-12
3. Convergent solid-phase peptide synthesis;Tetrahedron;1993-01
4. Membrane matrix for the hydrolysis of amino acid esters with marked enantioselectivity;Journal of the American Chemical Society;1988-03
5. Single-Centre Model for the Active Site of ?-Chymotrypsin;Helvetica Chimica Acta;1986-03-19
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