Fast collective motions of backbone in transmembrane α helices are critical to water transfer of aquaporin.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 38718112.
- Also identified by DOI 10.1126/sciadv.ade9520 and PMC identifier 11078191.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Fast collective motions are widely present in biomolecules, but their functional relevance remains unclear. Herein, we reveal that fast collective motions of backbone are critical to the water transfer of aquaporin Z (AqpZ) by using solid-state nuclear magnetic resonance (ssNMR) spectroscopy and molecular dynamics (MD) simulations. A total of 212 residue site-specific dipolar order parameters and 158 <sup>15</sup>N spin relaxation rates of the backbone are measured by combining the <sup>13</sup>C- and <sup>1</sup>H-detected multidimensional ssNMR spectra. Analysis of these experimental data by theoretic models suggests that the small-amplitude (~10°) collective motions of the transmembrane α helices on the nanosecond-to-microsecond timescales are dominant for the dynamics of AqpZ. The MD simulations demonstrate that these collective motions are critical to the water transfer efficiency of AqpZ by facilitating the opening of the channel and accelerating the water-residue hydrogen bonds renewing in the selectivity filter region.
Medical subject headings
- Water
- Aquaporins
- Molecular Dynamics Simulation