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
The Fourier synthesis of the crystal structure of strychnine sulphate pentahydrate
Journal ArticleDOI
The structure of carboxypeptidase A
William N. Lipscomb,J. C. Coppola,J.A. Hartsuck,M. L. Ludwig,H. Muirhead,J. Searl,Thomas A. Steitz +6 more
TL;DR: The molecular shape of carboxypeptidase Aα, a probable tracing of the polypeptide chain, estimation of the helical content as about 25% and the direct location of the zinc atom are presented.
Journal ArticleDOI
A Second Right-handed Helical Structure with the Parameters of the Pauling–Corey α-helix
TL;DR: In this paper, the authors predict bent hydrogen bonding between some CO and NH groups in the peptide chains of α-helices and X-ray crystallography has revealed the existence of such bonds in myoglobin and lysozyme.
Related Papers (5)
Metallocarboxypeptidases: stability constants and enzymatic characteristics.
Joseph E. Coleman,Bert L. Vallee +1 more