The accessible surface area and stability of oligomeric proteins.

Abstract:

:Protein structures are stabilized by hydrophobic and van der Waals forces, and by hydrogen bonds. The relation between these thermodynamic quantities and the actual three-dimensional structure of proteins can not be calculated precisely. However, certain empirical relations have been discovered. Hydrophobic energy is gained by the reduction of surface in contact with water. For monomeric proteins, the area of the surface accessible to solvent, and of that buried in the interior, is a simple function of molecular weight. Proteins with different shapes and secondary structures, but of the same molecular weight, have the same accessible surface area. It has been argued that there is no similar relationship for large oligomeric proteins. In this paper we show that the surface areas of oligomeric proteins, and the areas of the surface buried within them, are directly related to relative molecular mass. Although oligomers of the same molecular weight bury the same amounts of surface, the proportions buried within and between subunits vary. This has important implications for the role of subunit interfaces in the stability and activity of oligomeric proteins.

journal_name

Nature

journal_title

Nature

authors

Miller S,Lesk AM,Janin J,Chothia C

doi

10.1038/328834a0

subject

Has Abstract

pub_date

1987-08-27 00:00:00

pages

834-6

issue

6133

eissn

0028-0836

issn

1476-4687

journal_volume

328

pub_type

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