The interaction of D-Amino acid residues with the aromatic binding site of α-chymotrypsin
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(74)80098-0/fullpdf
Reference15 articles.
1. Structure of crystalline α-chymotrypsin
2. The Evaluation of the Enzyme-Inhibitor Dissociation Constants of α-Chymotrypsin and Several Pairs of Charged and Uncharged Competitive Inhibitors at pH 7.9 and 6.91,2
3. Re-evaluation of the Inhibition Constants of Previously Investigated Competitive Inhibitors of α-Chymotrypsin. II. Mono-, Bi- and Trifunctional Inhibitors Evaluated under Zone A Conditions1
4. The binding of inhibitors to α-chymotrypsin
5. Magnetic resonance studies of protein-small molecule interactions. Binding of N-trifluoroacetyl-D-(and L-)-p-fluorophenylalanine to .alpha.-chymotrypsin
Cited by 8 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. The 3′-End of tRNA and Its Role in Protein Biosynthesis;Angewandte Chemie International Edition in English;1985-05
2. Das 3′-Ende der tRNA und seine Rolle bei der Proteinbiosynthese;Angewandte Chemie;1985-05
3. Donor site of ribosomal peptidyltransferase: investigation of substrate specificity using 2'(3')-O-(N-acylaminoacyl)dinucleoside phosphates as models of the 3'-terminus of N-acylaminoacyl transfer ribonucleic acid;Biochemistry;1981-06-09
4. Stereochemical control of ribosomal peptidyltransferase reaction. Role of amino acid side-chain orientation of acceptor substrate;Biochemistry;1981-01-06
5. Inhibition of cathepsin D by synthetic oligopeptides.;Journal of Biological Chemistry;1979-12
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