期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 106, 期 25, 页码 10153-10158出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0904461106
关键词
energy landscape theory; protein folding; Rop dimer; single molecule FRET
资金
- National Institutes of Health [GM066833, GM083114]
- National Science Foundation [MCB-0543906, PHY-0750049]
- Center for Theoretical Biological Physics [PHY-0822283]
- La Jolla Interface in Science Program postdoctoral fellowship
- Great Rivers Affiliate of the American Heart Association predoctoral fellowship
- National Institute of Neurological Disorders and Stroke/National Institutes of Health postdoctoral fellowship
Biological activity in proteins requires them to share the energy landscape for folding and global conformational motions, 2 key determinants of function. Although most structural studies to date have focused on fluctuations around a single structural basin, we directly observe the coexistence of 2 symmetrically opposed conformations for a mutant of the Rop-homodimer ( Repressor of Primer) in single-molecule fluorescence resonance energy transfer (smFRET) measurements. We find that mild denaturing conditions can affect the sensitive balance between the conformations, generating an equilibrium ensemble consisting of 2 equally occupied structural basins. Despite the need for large-scale conformational rearrangement, both native structures are dynamically and reversibly adopted for the same paired molecules without separation of the constituent monomers. Such an ability of some proteins or protein complexes to switch between conformations by thermal fluctuations and/or minor environmental changes could be central to their ability to control biological function.
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