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 language | English (US) |
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Pages (from-to) | 4-10 |
Number of pages | 7 |
Journal | Current Opinion in Structural Biology |
Volume | 23 |
Issue number | 1 |
DOIs | |
State | Published - Feb 2013 |
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology