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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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Journal ArticleDOI

Dynamics of folded proteins

TL;DR: The dynamics of a folded globular protein have been studied by solving the equations of motion for the atoms with an empirical potential energy function and suggest that the protein interior is fluid-like in that the local atom motions have a diffusional character.
Journal ArticleDOI

The internal dynamics of globular proteins.

TL;DR: The Internal Dynamics of Globular Protein (IDGP) as mentioned in this paper is a well-known model for the internal dynamics of protein structures and its dynamics in the context of protein synthesis.
Book ChapterDOI

Carboxypeptidase A: a protein and an enzyme.

TL;DR: This chapter discusses the relationship of the three-dimensional structures of bovine carboxypeptidase A, and of its complexes with substrates and inhibitors, to the functional behavior of this enzyme.
References
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Journal ArticleDOI

New structural model of E. coli aspartate transcarbamylase and the amino-acid sequence of the regulatory polypeptide chain.

TL;DR: Molecular weight determinations of the regulatory and catalytic chains and the amino-acid sequence of the R chain indicate that the ATCase molecule contains six copies of each chain.
Journal ArticleDOI

Crystallographic determination of symmetry of aspartate transcarbamylase.

TL;DR: Studies of trigonal and tetragonal crystalline forms of aspartate transcarbamylase show that the molecule has a three-fold and a two-fold symmetry axis.
Journal ArticleDOI

On the size of the active site in proteases. II. Carboxypeptidase-A.

TL;DR: In this paper, the size of the active site of carboxypeptidase-A was investigated by studying the kinetics of hydrolysis of peptides of L-alanine, Dalanine and L-phenylalanine.
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