Abstract
Membrane proteins change their conformations in response to chemical and physical stimuli and transmit extracellular signals inside cells. Several approaches have been developed for solving the structures of proteins. However, few techniques can monitor real-time protein dynamics. The diffracted X-ray tracking method (DXT) is an X-ray-based single-molecule technique that monitors the internal motion of biomolecules in an aqueous solution. DXT analyzes trajectories of Laue spots generated from the attached gold nanocrystals with a two-dimensional axis by tilting (θ) and twisting (χ). Furthermore, high-intensity X-rays from synchrotron radiation facilities enable measurements with microsecond-timescale and picometer-spatial-scale intramolecular information. The technique has been applied to various membrane proteins due to its superior spatiotemporal resolution. In this review, we introduce basic principles of DXT, reviewing its recent and extended applications to membrane proteins and living cells, respectively.
Highlights
Recent advances in cryo-electron microscopy have revealed structural information for various membrane proteins or supramolecular complexes at near atomic resolution that have been difficult to crystallize or inapplicable to NMR and in silico analysis, due to size limitation [1]
Several single-molecule techniques have been applied to understand the dynamics of membrane proteins
We focus on diffracted X-ray tracking (DXT) techniques for their high-resolution angular displacemonitoring of the internal motion of protein molecules requires precision at the picometer ment and temporal resolution with microsecond-to-millisecond order
Summary
Recent advances in cryo-electron microscopy have revealed structural information for various membrane proteins or supramolecular complexes at near atomic resolution that have been difficult to crystallize or inapplicable to NMR and in silico analysis, due to size limitation [1]. We focus on DXT techniques for their high-resolution angular displacemonitoring of the internal motion of protein molecules requires precision at the picometer ment and temporal resolution with microsecond-to-millisecond order. Accurate monitoring level, which is three orders of magnitude lower than the nanometer level This can be of the internal motion of protein molecules requires precision at the picometer level, which achieved not by visible light but with X-rays. The positioning accuracy of single molecule is three orders of magnitude lower than the nanometer level This can be achieved not by measurements is possible up to λ/100, where λ is the wavelength. DXT uses broadband X-rays (a white or pink beam) instead of a monochromatic X-ray as the irradiation source This enables us to track the angular displacement of the diffraction spots from individual gold nanocrystals (Figure 1B).
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