Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 53, Issue 9, Pages 2358-2361Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201308512
Keywords
acyl carrier protein; folding intermediates; protein dynamics; protein folding; protein structure
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Funding
- Singapore Ministry of Education (Academic Research Fund Tier 3) [MOE2012-T3-1-008]
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A protein can exist in multiple states under native conditions and those states with low populations are often critical to biological function and self-assembly. To investigate the role of the minor states of an acyl carrier protein, NMR techniques were applied to determine the number of minor states and characterize their structures and kinetics. The acyl carrier protein from Micromonospora echinospora was found to exist in one major folded state (95.2%), one unfolded state (4.1%), and one intermediate state (0.7%) under native conditions. The three states are in dynamic equilibrium and the intermediate state very likely adopts a native-like structure and is an off-pathway folding product. The intermediate state may mediate the formation of oligomers invitro and play an important role in the recognition of partner enzymes invivo.
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