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Journal ArticleDOI

Structure and mechanism in the enzymic activity of carboxypeptidase A and relations to chemical sequence

William N. Lipscomb
- 01 Mar 1970 - 
- Vol. 3, Iss: 3, pp 81-89
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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.

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Citations
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Oligomers and Cyclooligomers of Rigid Phenylene–Ethynylene–Butadiynylenes: Synthesis and Self-Assembled Monolayers†

TL;DR: This study was motivated by the question as to whether these oligomers can form stable SAMs at the solid/liquid interface that can be investigated by STM, and presented a series of acyclic and cyclic phenylene–ethynylene–butadiynylene(PEB) oligomers prepared by oxidative acetylene oligomers.
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Resolution of optical isomers of Dns-amino acids by high-performance liquid chromatography with l-histidine and its derivatives in the mobile phase

TL;DR: In this article, the optical isomers of Dns-amino acids were resolved by high-performance liquid chromatography with mixed chelate complexation, including aliphatic, polar and aromatic substituents.
Journal ArticleDOI

A model for ZnII-containing-β-lactamase: synthesis, X-ray crystal structure of a zinc(II) complex bearing thiol groupand hydrolysis of phosphate diester

TL;DR: A novel N3S1 typed tripodal ligand bearing an SH group, N-(mercaptoethyl)-di(2-pyridylmethyl)amine, DPASH, was prepared and its zinc(II) complex, [ZnII(DPAS)Cl], was structurally characterized by X-ray crystallography.
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Metal Ion Catalysis in the Hydrolysis of Esters of 2-Hydroxy-1,10-phenanthroline: The Effects of Metal Ions on Intramolecular Carboxyl Group Participation.

TL;DR: These are the most rapid neighboring carboxyl group reactions that have been observed in ester hydrolysis, which allows the neighboring group reaction to be competitive with the favorable metal ion-promoted OH(-) reaction at pH < 6, but not at pH > 6.
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Structure and internal mobility of proteins: a molecular dynamics study of hen egg white lysozyme.

TL;DR: The structure and internal motions of the protein hen egg white lysozyme are studied by analysis of simulation and experimental data and the regions that have large deviations among the x‐ray crystal structures, which indicates flexibility, are found to have large fluctuations in the simulation.
References
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Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution.

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 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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