Abstract
Since natural proteins are the products of a long evolutionary process, the structural properties of present-day proteins should depend not only on physico-chemical constraints, but also on evolutionary constraints. Here we propose a model for protein evolution, in which membranes play a key role as a scaffold for supporting the gradual evolution from flexible polypeptides to well-folded proteins. We suggest that the folding process of present-day globular proteins is a relic of this putative evolutionary process. To test the hypothesis that membranes once acted as a cradle for the folding of globular proteins, extensive research on membrane proteins and the interactions of globular proteins with membranes will be required.
| Original language | English |
|---|---|
| Pages (from-to) | 150-153 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 430 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 1998 Jul 3 |
| Externally published | Yes |
Keywords
- Exon shuffling
- Membrane-bound enzyme
- Molecular chaperone
- Molten globule state
- Protein evolution
- Protein folding
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
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