Journal ArticleDOI
Structure and mechanism in the enzymic activity of carboxypeptidase A and relations to chemical sequence
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This article is published in Accounts of Chemical Research.The article was published on 1970-03-01. It has received 126 citations till now. The article focuses on the topics: Carboxypeptidase A & Carboxypeptidase.read more
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Mixed Ligand Copper(II) Complexes of α-Amino Acids with Ligand-Ligand Interactions
TL;DR: For all combinations of ligands A and B, where A refers to aspartic or glutamic acid and B to arginine, lysine, or ornithine, the mixed ligand complexes, [Cu(L-A)(L-B), [C-L-Aspartate), [D-A, L-B], and [C -L-Lornithine], were isolated as crystals, whereas no such enhancement was observed when one of the ligands was L-alanine or L-valine as mentioned in this paper.
Journal ArticleDOI
Protein conformational transitions in the erythrocyte membrane
TL;DR: Using infrared absorption spectroscopy, it is demonstrated that in the presence of adenosine triphosphate and Mg 2+ , the protein in these membranes undergoes a transition to an anti-parallel β structure, which is enhanced by the addition of Na + and K + .
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Hydrolytic metalloenzyme models. Micellar effects on the activation of the hydroxyl groups of N-alkyl-2-(hydroxymethyl)-imidazole ligands by Cu2+ in the transacylation of p-nitrophenyl picolinate.
TL;DR: The kinetic analyses indicated that the 1:1 and 2:1 complexes of the ligand and Cu2+ are active nucleophiles with the N-methyl and N-dodecyl ligand, respectively.
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Weak interactions in metal complexes of amino acids with a phosphorylated side chain. Conversion of aromatic ring stacking to electrostatic bonding by tyrosine phosphorylation
TL;DR: In this article, the stability of ternary Cu(II) complexes with the phosphoesters of amino acids (A=Ophosphoserine (Pser) or I=0.1 and 1.0 M(KNO3) ) was evaluated by calculating the equilibrium constant K for the following hypothetical equilibrium from the overall stability constant of each Ternary species:, where A′ refers to serine or tyrosine (Tyr) and B′ to alanine and the interactions are possible only in CU(L-A)(L-B
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Chemical evidence for a functional carboxyl group in carboxypeptidase A
TL;DR: Modification of carboxypeptidase A with 1-cyclohexyl-3-(2-morpholinoethyl)-carbodiimide metho-p-toluene sulfonate at pH 6.0 simultaneously abolishes both esterase and peptidase activities.
References
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Journal ArticleDOI
Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution.
C. C. F. Blake,D. F. Koenig,D. F. Koenig,G. A. Mair,A. C. T. North,D. C. Phillips,V. R. Sarma +6 more
TL;DR: Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 A Resolution as mentioned in this paper, 3D Fourier synthesis at 2 a resolution.
Journal ArticleDOI
Structure of Myoglobin: A Three-Dimensional Fourier Synthesis at 2 Å. Resolution
J. C. Kendrew,R. E. Dickerson,B. E. Strandberg,R G Hart,D R Davies,D. C. Phillips,V. C. Shore +6 more
Journal ArticleDOI
Structure of papain.
TL;DR: A three-dimensional X-ray study at a resolution of 2.8 A has revealed that the single polypeptide chain of 211 residues is folded into two distinct parts which are divided by a cleft as mentioned in this paper.
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