The quaternary structure of proteins composed of identical subunits.

Abstract The possible structures which could arise on assembly of identical subunits into oligomeric structures have been made by assuming (a) that these are closed structures, (b) that whatever conformational changes occur on association are the same for each subunit, and (c) that there is no a priori reason for preferring a particular type of binding domain. When such an analysis is applied to dimers, trimers, and tetramers, it is seen that structures with heterologous binding sites are as likely as structures with isologous binding sites if thermodynamic considerations alone are relevant. Proteins with mixed isologous and heterologous binding sites are also found to be possible under some circumstances assuming possible values for subunit interaction constants. An analysis of the quantities of trimers, dimers, and monomers produced on dissociation of a tetramer shows that certain limits can be placed on the amounts of the dissociated species based on the possible protein structures. These limits therefore provide possible diagnostic tests for exploring protein design.

• Publication year

  1971

• Venue

  Journal of Biological Chemistry

• Publication date

  1971-05-25

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/s0021-9258(18)62200-8PMID 5574388
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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