Journal
NATURE CHEMICAL BIOLOGY
Volume 9, Issue 5, Pages 313-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.1213
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Funding
- Pioneer Research Program for Converging Technology [2008-2000218]
- Advanced Biomass RD Center [2011-0031363]
- Intelligent Synthetic Biology Center [2011-0031950]
- Brain Korea 21 program of the Ministry of Education, Science and Technology and Creative Research Initiatives [2009-0081562]
- World-Class University program of the National Research Foundation of Kore
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Protein dynamics have been suggested to have a crucial role in biomolecular recognition, but the precise molecular mechanisms remain unclear. Herein, we performed single-molecule fluorescence resonance energy transfer measurements for wild-type maltose-binding protein (MBP) and its variants to demonstrate the interplay of conformational dynamics and molecular recognition. Kinetic analysis provided direct evidence that MBP recognizes a ligand through an 'induced-fit' mechanism, not through the generally proposed selection mechanism for proteins with conformational dynamics such as MBP. Our results indicated that the mere presence of intrinsic dynamics is insufficient for a 'selection' mechanism. An energetic analysis of ligand binding implicated the critical role of conformational dynamics in facilitating a structural change that occurs upon ligand binding.
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