Forces and factors that contribute to the structural stability of membrane proteins

Tuomas Haltia, Ernesto Freire

Research output: Contribution to journalReview articlepeer-review

139 Scopus citations


While a considerable amount of literature deals with the structural energetics of water-soluble proteins, relatively little is known about the forces that determine the stability of membrane proteins. Similarly, only a few membrane protein structures are known at atomic resolution, although new structures have recently been described. In this article, we review the current knowledge about the structural features of membrane proteins. We then proceed to summarize the existing literature regarding the thermal stability of bacteriorhodopsin, cytochrome-c oxidase, the band 3 protein, Photosystem II and porins. We conclude that a fundamental difference between soluble and membrane proteins is the high thermal stability of intrabilayer secondary structure elements in membrane proteins. This property manifests itself as incomplete unfolding, and is reflected in the observed low enthalpies of denaturation of most membrane proteins. By contrast, the extramembranous parts of membrane proteins may behave much like soluble proteins. A brief general account of thermodynamics factors that contribute to the stability of water soluble and membrane proteins is presented.

Original languageEnglish (US)
Pages (from-to)1-27
Number of pages27
JournalBBA - Bioenergetics
Issue number1
StatePublished - Feb 14 1995


  • Bacteriorhodopsin
  • Band 3 protein
  • Calorimetry
  • Cytochrome oxidase
  • Photosystem II
  • Thermal stability

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology


Dive into the research topics of 'Forces and factors that contribute to the structural stability of membrane proteins'. Together they form a unique fingerprint.

Cite this