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Visualizing Intramolecular Dynamics of Membrane Proteins

Membrane proteins play important roles in biological functions, with accompanying allosteric structure changes. Understanding intramolecular dynamics helps elucidate catalytic mechanisms and develop new drugs. In contrast to the various technologies for structural analysis, methods for analyzing int...

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Detalles Bibliográficos
Autores principales: Ohkubo, Tatsunari, Shiina, Takaaki, Kawaguchi, Kayoko, Sasaki, Daisuke, Inamasu, Rena, Yang, Yue, Li, Zhuoqi, Taninaka, Keizaburo, Sakaguchi, Masaki, Fujimura, Shoko, Sekiguchi, Hiroshi, Kuramochi, Masahiro, Arai, Tatsuya, Tsuda, Sakae, Sasaki, Yuji C., Mio, Kazuhiro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9736139/
https://www.ncbi.nlm.nih.gov/pubmed/36498865
http://dx.doi.org/10.3390/ijms232314539
Descripción
Sumario:Membrane proteins play important roles in biological functions, with accompanying allosteric structure changes. Understanding intramolecular dynamics helps elucidate catalytic mechanisms and develop new drugs. In contrast to the various technologies for structural analysis, methods for analyzing intramolecular dynamics are limited. Single-molecule measurements using optical microscopy have been widely used for kinetic analysis. Recently, improvements in detectors and image analysis technology have made it possible to use single-molecule determination methods using X-rays and electron beams, such as diffracted X-ray tracking (DXT), X-ray free electron laser (XFEL) imaging, and cryo-electron microscopy (cryo-EM). High-speed atomic force microscopy (HS-AFM) is a scanning probe microscope that can capture the structural dynamics of biomolecules in real time at the single-molecule level. Time-resolved techniques also facilitate an understanding of real-time intramolecular processes during chemical reactions. In this review, recent advances in membrane protein dynamics visualization techniques were presented.