Molten globules, entropy-driven conformational change and protein folding

Robert L. Baldwin, George D. Rose

Research output: Contribution to journalReview article

Abstract

The exquisite side chain close-packing in the protein core and at binding interfaces has prompted a conviction that packing selectivity is the primary mechanism for molecular recognition in folding and/or binding reactions. Contrary to this view, molten globule proteins can adopt native topology and bind targets tightly and specifically in the absence of side chain close-packing. The molten globule is a highly dynamic form with native-like secondary structure and a loose protein core that admits solvent. The related (but still controversial) dry molten globule is an expanded form of the native protein with largely intact topology but a tighter protein core that excludes solvent. Neither form retains side chain close-packing, and therefore both structure and function must result from other factors, assuming that the reality of the dry molten globule is accepted. This simplifying realization calls for a re-evaluation of established models.

Original languageEnglish (US)
Pages (from-to)4-10
Number of pages7
JournalCurrent Opinion in Structural Biology
Volume23
Issue number1
DOIs
StatePublished - Feb 1 2013

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ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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