Origins of globular structure in proteins

Nobuhide Doi, Hiroshi Yanagawa

Research output: Contribution to journalArticle

12 Citations (Scopus)

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 languageEnglish
Pages (from-to)150-153
Number of pages4
JournalFEBS Letters
Volume430
Issue number3
DOIs
Publication statusPublished - 1998 Jul 3
Externally publishedYes

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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