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
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
Synthetic analogues relevant to the structure and function of zinc enzymes.
Journal ArticleDOI
Analog approaches to the structure of the transition state in enzyme reactions
Journal ArticleDOI
The internal dynamics of globular proteins.
Martin Karplus,J. A. McCammon +1 more
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
Kinetics of Carboxypeptidase Action. I. Effect of Various Extrinsic Factors on Kinetic Parameters1
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Metallocarboxypeptidases: stability constants and enzymatic characteristics.
Joseph E. Coleman,Bert L. Vallee +1 more
Journal ArticleDOI
Crystallographic determination of symmetry of aspartate transcarbamylase.
Don C. Wiley,William N. Lipscomb +1 more
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.
Related Papers (5)
Metallocarboxypeptidases: stability constants and enzymatic characteristics.
Joseph E. Coleman,Bert L. Vallee +1 more