Diffracted X-ray Tracking Method for Measuring Intramolecular Dynamics of Membrane Proteins
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-r...
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| Published in: | International journal of molecular sciences Vol. 23; no. 4; p. 2343 |
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| Main Authors: | , , , , , , |
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| 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 (
) and twisting (
). 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. |
|---|---|
| AbstractList | 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. 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. 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 ( ) and twisting ( ). 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. |
| Author | Fujimura, Shoko Mio, Kazuhiro Ohkubo, Tatsunari Kuramochi, Masahiro Sekiguchi, Hiroshi Arai, Tatsuya Sasaki, Yuji C |
| AuthorAffiliation | 5 Center for Synchrotron Radiation Research, Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo-cho, Sayo 679-5198, Japan; sekiguchi@spring8.or.jp 3 Graduate School of Frontier Sciences, The University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa 277-8561, Japan; t.arai@edu.k.u-tokyo.ac.jp (T.A.); masahiro.kuramochi.vw26@vc.ibaraki.ac.jp (M.K.) 1 AIST-UTokyo Advanced Operando-Measurement Technology Open Innovation Laboratory (OPERANDO-OIL), National Institute of Advanced Industrial Science and Technology (AIST), 6-2-3 Kashiwanoha, Kashiwa 277-0882, Japan; shoko-san@aist.go.jp (S.F.); i180125b@yokohama-cu.ac.jp (T.O.) 4 Graduate School of Science and Engineering, Ibaraki University, Hitachi 316-8511, Japan 2 Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan |
| AuthorAffiliation_xml | – name: 5 Center for Synchrotron Radiation Research, Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo-cho, Sayo 679-5198, Japan; sekiguchi@spring8.or.jp – name: 2 Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan – name: 3 Graduate School of Frontier Sciences, The University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa 277-8561, Japan; t.arai@edu.k.u-tokyo.ac.jp (T.A.); masahiro.kuramochi.vw26@vc.ibaraki.ac.jp (M.K.) – name: 4 Graduate School of Science and Engineering, Ibaraki University, Hitachi 316-8511, Japan – name: 1 AIST-UTokyo Advanced Operando-Measurement Technology Open Innovation Laboratory (OPERANDO-OIL), National Institute of Advanced Industrial Science and Technology (AIST), 6-2-3 Kashiwanoha, Kashiwa 277-0882, Japan; shoko-san@aist.go.jp (S.F.); i180125b@yokohama-cu.ac.jp (T.O.) |
| Author_xml | – sequence: 1 givenname: Shoko surname: Fujimura fullname: Fujimura, Shoko organization: AIST-UTokyo Advanced Operando-Measurement Technology Open Innovation Laboratory (OPERANDO-OIL), National Institute of Advanced Industrial Science and Technology (AIST), 6-2-3 Kashiwanoha, Kashiwa 277-0882, Japan – sequence: 2 givenname: Kazuhiro orcidid: 0000-0002-1655-8231 surname: Mio fullname: Mio, Kazuhiro organization: Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan – sequence: 3 givenname: Tatsunari surname: Ohkubo fullname: Ohkubo, Tatsunari organization: Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan – sequence: 4 givenname: Tatsuya surname: Arai fullname: Arai, Tatsuya organization: Graduate School of Frontier Sciences, The University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa 277-8561, Japan – sequence: 5 givenname: Masahiro orcidid: 0000-0003-1643-3997 surname: Kuramochi fullname: Kuramochi, Masahiro organization: Graduate School of Science and Engineering, Ibaraki University, Hitachi 316-8511, Japan – sequence: 6 givenname: Hiroshi orcidid: 0000-0001-7590-3624 surname: Sekiguchi fullname: Sekiguchi, Hiroshi organization: Center for Synchrotron Radiation Research, Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo-cho, Sayo 679-5198, Japan – sequence: 7 givenname: Yuji C orcidid: 0000-0003-3403-237X surname: Sasaki fullname: Sasaki, Yuji C organization: Center for Synchrotron Radiation Research, Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo-cho, Sayo 679-5198, Japan |
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| Cites_doi | 10.1103/PhysRevE.70.021917 10.1021/acscatal.5b00331 10.1038/nature12823 10.1021/jacs.6b03496 10.1016/j.tsf.2004.04.033 10.1021/bc100429d 10.1038/nature12822 10.1021/ja407265p 10.1016/j.bbrc.2017.01.165 10.1038/s41598-021-92986-3 10.1038/srep06384 10.1038/nature19948 10.3109/08820137809033919 10.1126/scisignal.aao1917 10.1016/j.bbrc.2020.05.200 10.1016/j.cell.2007.11.040 10.1103/PhysRevLett.87.248102 10.1038/s41598-018-35468-3 10.3390/ijms22105285 10.1016/S0006-3495(97)78830-1 10.1016/j.bbrc.2021.03.144 10.1088/1748-0221/10/01/T01002 10.1002/cbic.202100106 10.1007/s00424-007-0406-0 10.1073/pnas.1814277115 10.1002/cphc.201300880 10.1021/acs.jpcb.0c08250 10.1103/PhysRevE.62.3843 10.1038/s41598-021-83320-y 10.1021/acsnano.7b03447 10.1038/nsmb.3138 10.3390/ijms22168473 10.1371/journal.pone.0064176 10.1063/4.0000112 10.1021/ja506231j |
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| References | Ando (ref_11) 2008; 456 Sasaki (ref_18) 2000; 62 Sasmal (ref_34) 2014; 136 Katoh (ref_10) 2021; 11 ref_13 Liao (ref_26) 2013; 504 Sekiguchi (ref_14) 2014; 4 Kuramochi (ref_32) 2021; 11 Okada (ref_23) 2011; 22 Sasmal (ref_35) 2016; 138 Gicheru (ref_28) 2018; 115 Yanagawa (ref_6) 2018; 11 Bartels (ref_5) 2021; 22 Okumura (ref_20) 2004; 70 Chang (ref_30) 2021; 556 Scheres (ref_1) 2016; 537 Wang (ref_4) 2016; 23 ref_17 Mio (ref_16) 2020; 529 Sasaki (ref_22) 1997; 72 Backlund (ref_8) 2014; 15 Fujimura (ref_15) 2020; 124 Okumura (ref_21) 2005; 471 Cao (ref_27) 2013; 504 Shimizu (ref_12) 2008; 132 Sasaki (ref_19) 2001; 87 Singh (ref_2) 2015; 5 Hemonnot (ref_29) 2017; 11 Geoghegan (ref_24) 1978; 7 Fujimura (ref_9) 2017; 485 Yagi (ref_25) 2015; 10 Arai (ref_33) 2021; 8 Brust (ref_3) 2013; 135 ref_7 Sekiguchi (ref_31) 2018; 8 |
| References_xml | – volume: 70 start-page: 021917 year: 2004 ident: ref_20 article-title: Picometer-scale dynamical observations of individual membrane proteins: The case of bacteriorhodopsin publication-title: Phys. Rev. E doi: 10.1103/PhysRevE.70.021917 contributor: fullname: Okumura – volume: 5 start-page: 3067 year: 2015 ident: ref_2 article-title: Network of remote and local protein dynamics in dihydrofolate reductase catalysis publication-title: ACS Catal. doi: 10.1021/acscatal.5b00331 contributor: fullname: Singh – volume: 504 start-page: 113 year: 2013 ident: ref_27 article-title: TRPV1 structures in distinct conformations reveal activation mechanisms publication-title: Nature doi: 10.1038/nature12823 contributor: fullname: Cao – volume: 138 start-page: 8789 year: 2016 ident: ref_35 article-title: Single-Molecule Patch-Clamp FRET Anisotropy Microscopy Studies of NMDA Receptor Ion Channel Activation and Deactivation under Agonist Ligand Binding in Living Cells publication-title: J. Am. Chem. Soc. doi: 10.1021/jacs.6b03496 contributor: fullname: Sasmal – volume: 471 start-page: 91 year: 2005 ident: ref_21 article-title: Fabrications of dispersive gold one-dimensional nanocrystals using vacuum evaporation publication-title: Thin Solid Film. doi: 10.1016/j.tsf.2004.04.033 contributor: fullname: Okumura – volume: 22 start-page: 887 year: 2011 ident: ref_23 article-title: New Protein Purification System Using Gold-Magnetic Beads and a Novel Peptide Tag, “the Methionine Tag” publication-title: Bioconjug. Chem. doi: 10.1021/bc100429d contributor: fullname: Okada – volume: 504 start-page: 107 year: 2013 ident: ref_26 article-title: Structure of the TRPV1 ion channel determined by electron cryo-microscopy publication-title: Nature doi: 10.1038/nature12822 contributor: fullname: Liao – volume: 135 start-page: 16168 year: 2013 ident: ref_3 article-title: Proteins in action: Femtosecond to millisecond structural dynamics of a photoactive flavoprotein publication-title: J. Am. Chem. Soc. doi: 10.1021/ja407265p contributor: fullname: Brust – volume: 485 start-page: 614 year: 2017 ident: ref_9 article-title: Dissection of the angle of single fluorophore attached to the nucleotide in corkscrewing microtubules publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2017.01.165 contributor: fullname: Fujimura – volume: 11 start-page: 13672 year: 2021 ident: ref_10 article-title: Angle change of the A-domain in a single SERCA1a molecule detected by defocused orientation imaging publication-title: Sci. Rep. doi: 10.1038/s41598-021-92986-3 contributor: fullname: Katoh – volume: 4 start-page: 6384 year: 2014 ident: ref_14 article-title: Real time ligand-induced motion mappings of AChBP and nAChR using X-ray single molecule tracking publication-title: Sci. Rep. doi: 10.1038/srep06384 contributor: fullname: Sekiguchi – volume: 537 start-page: 339 year: 2016 ident: ref_1 article-title: Unravelling biological macromolecules with cryo-electron microscopy publication-title: Nature doi: 10.1038/nature19948 contributor: fullname: Scheres – volume: 7 start-page: 1 year: 1978 ident: ref_24 article-title: The detection of human B lymphocytes by both light and electron microscopy utilizing colloidal gold labeled anti-immunoglobulin publication-title: Immunol. Commun. doi: 10.3109/08820137809033919 contributor: fullname: Geoghegan – volume: 11 start-page: eaao1917 year: 2018 ident: ref_6 article-title: Single-molecule diffusion-based estimation of ligand effects on G protein-coupled receptors publication-title: Sci. Signal. doi: 10.1126/scisignal.aao1917 contributor: fullname: Yanagawa – volume: 529 start-page: 306 year: 2020 ident: ref_16 article-title: X-ray-based living-cell motion analysis of individual serotonin receptors publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2020.05.200 contributor: fullname: Mio – volume: 132 start-page: 67 year: 2008 ident: ref_12 article-title: Global twisting motion of single molecular KcsA potassium channel upon gating publication-title: Cell doi: 10.1016/j.cell.2007.11.040 contributor: fullname: Shimizu – volume: 87 start-page: 248102 year: 2001 ident: ref_19 article-title: Picometer-scale dynamical x-ray imaging of single DNA molecules publication-title: Phys. Rev. Lett. doi: 10.1103/PhysRevLett.87.248102 contributor: fullname: Sasaki – volume: 8 start-page: 17090 year: 2018 ident: ref_31 article-title: Diffracted X-ray Blinking Tracks Single Protein Motions publication-title: Sci. Rep. doi: 10.1038/s41598-018-35468-3 contributor: fullname: Sekiguchi – ident: ref_17 doi: 10.3390/ijms22105285 – volume: 72 start-page: 1842 year: 1997 ident: ref_22 article-title: Two-dimensional arrangement of a functional protein by cysteine-gold interaction: Enzyme activity and characterization of a protein monolayer on a gold substrate publication-title: Biophys. J. doi: 10.1016/S0006-3495(97)78830-1 contributor: fullname: Sasaki – volume: 556 start-page: 53 year: 2021 ident: ref_30 article-title: Diffracted X-ray blinking measurements of interleukin 15 receptors in the inner/outer membrane of living NK cells publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2021.03.144 contributor: fullname: Chang – volume: 10 start-page: T01002 year: 2015 ident: ref_25 article-title: An X-ray image intensifier for microsecond time-resolved experiments publication-title: J. Instrum. doi: 10.1088/1748-0221/10/01/T01002 contributor: fullname: Yagi – volume: 22 start-page: 2657 year: 2021 ident: ref_5 article-title: Single-Molecule FRET of Membrane Transport Proteins publication-title: Chembiochem doi: 10.1002/cbic.202100106 contributor: fullname: Bartels – volume: 456 start-page: 211 year: 2008 ident: ref_11 article-title: High-speed AFM and nano-visualization of biomolecular processes publication-title: Pflug. Arch. doi: 10.1007/s00424-007-0406-0 contributor: fullname: Ando – volume: 115 start-page: 10198 year: 2018 ident: ref_28 article-title: Direct visualization of ion-channel gating in a native environment publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1814277115 contributor: fullname: Gicheru – volume: 15 start-page: 587 year: 2014 ident: ref_8 article-title: The role of molecular dipole orientation in single-molecule fluorescence microscopy and implications for super-resolution imaging publication-title: Chemphyschem doi: 10.1002/cphc.201300880 contributor: fullname: Backlund – volume: 124 start-page: 11617 year: 2020 ident: ref_15 article-title: Agonist and Antagonist-Diverted Twisting Motions of a Single TRPV1 Channel publication-title: J. Phys. Chem. B doi: 10.1021/acs.jpcb.0c08250 contributor: fullname: Fujimura – volume: 62 start-page: 3843 year: 2000 ident: ref_18 article-title: Tracking of individual nanocrystals using diffracted x rays publication-title: Phys. Rev. E doi: 10.1103/PhysRevE.62.3843 contributor: fullname: Sasaki – volume: 11 start-page: 4097 year: 2021 ident: ref_32 article-title: Tilting and rotational motions of silver halide crystal with diffracted X-ray blinking publication-title: Sci. Rep. doi: 10.1038/s41598-021-83320-y contributor: fullname: Kuramochi – volume: 11 start-page: 8542 year: 2017 ident: ref_29 article-title: Imaging of Biological Materials and Cells by X-ray Scattering and Diffraction publication-title: ACS Nano doi: 10.1021/acsnano.7b03447 contributor: fullname: Hemonnot – volume: 23 start-page: 31 year: 2016 ident: ref_4 article-title: Structural dynamics of potassium-channel gating revealed by single-molecule FRET publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb.3138 contributor: fullname: Wang – ident: ref_7 doi: 10.3390/ijms22168473 – ident: ref_13 doi: 10.1371/journal.pone.0064176 – volume: 8 start-page: 044302 year: 2021 ident: ref_33 article-title: Laboratory diffracted x-ray blinking to monitor picometer motions of protein molecules and application to crystalline materials publication-title: Struct. Dyn. doi: 10.1063/4.0000112 contributor: fullname: Arai – volume: 136 start-page: 12998 year: 2014 ident: ref_34 article-title: Single-molecule patch-clamp FRET microscopy studies of NMDA receptor ion channel dynamics in living cells: Revealing the multiple conformational states associated with a channel at its electrical off state publication-title: J. Am. Chem. Soc. doi: 10.1021/ja506231j contributor: fullname: Sasmal |
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| SubjectTerms | Accuracy Antibodies Aqueous solutions Binding sites Biomolecules conformation dynamics diffracted X-ray tracking technique Diffraction Gold - chemistry Measurement methods Membrane Proteins Membranes Microscopy Motion Nanocrystals Nanotechnology Peptides Potassium Proteins Radiation Radiation measurement Review single molecule analysis Synchrotron radiation Synchrotrons Trajectory analysis X-Ray Diffraction X-Rays |
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| Title | Diffracted X-ray Tracking Method for Measuring Intramolecular Dynamics of Membrane Proteins |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/35216461 https://www.proquest.com/docview/2632978847 https://search.proquest.com/docview/2633859146 https://pubmed.ncbi.nlm.nih.gov/PMC8880040 https://doaj.org/article/07a04f150b794de586f6b9d0d23eea2d |
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