Stereochemistry of oligomeric proteins

John Devens Gust, Gary Dirks

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

The subunits of many oligomeric proteins are organized into stable arrays with high symmetry. When these proteins interact with small molecules such as enzyme substrates or inhibitors, a variety of non-equivalent forms of the protein may be produced. Some of these forms have the same atomic composition, but differ in the spatial arrangement of the subunits. These species differ in all of their properties (conformation, affinity for substrate, etc.), and the relationships among them and among their subunits may be defined using stereochemical nomenclature which has been developed for small molecules. In many cases, the number of such forms is quite large. Rigorous, group-theoretical methods for enumerating all possible species are described and illustrated for the enzyme aspartate transcarbamoylase.

Original languageEnglish
Pages (from-to)39-55
Number of pages17
JournalJournal of Theoretical Biology
Volume92
Issue number1
DOIs
Publication statusPublished - Sep 7 1981

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Stereochemistry
stereochemistry
Proteins
Protein
Enzymes
aspartate carbamoyltransferase
Substrate
Molecules
proteins
enzyme substrates
enzyme inhibitors
Substrates
Terminology
Conformation
Aspartic Acid
Inhibitor
Affine transformation
Conformations
Arrangement
Symmetry

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)

Cite this

Stereochemistry of oligomeric proteins. / Gust, John Devens; Dirks, Gary.

In: Journal of Theoretical Biology, Vol. 92, No. 1, 07.09.1981, p. 39-55.

Research output: Contribution to journalArticle

Gust, John Devens ; Dirks, Gary. / Stereochemistry of oligomeric proteins. In: Journal of Theoretical Biology. 1981 ; Vol. 92, No. 1. pp. 39-55.
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