Category Ranking

98%

Total Visits

921

Avg Visit Duration

2 minutes

Citations

20

Article Abstract

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.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9736139PMC
http://dx.doi.org/10.3390/ijms232314539DOI Listing

Publication Analysis

Top Keywords

intramolecular dynamics
12
membrane proteins
8
dynamics
5
visualizing intramolecular
4
dynamics membrane
4
proteins membrane
4
proteins play
4
play roles
4
roles biological
4
biological functions
4

Similar Publications

We combined circular dichroism (CD) and viscosity measurements with molecular dynamics (MD) simulations and classification and regression approaches to machine learning to characterize solution structures of 22-mer, 25-mer, and 30-mer peptide- (-GlyArg6) conjugated phosphorodiamidate morpholino oligonucleotides (PPMOs). PPMO molecules form non-canonical folded structures with 1.4- to 1.

View Article and Find Full Text PDF

Unveiling photophysical mechanisms of NIR-II AIE luminogens for multimodal imaging-navigated synergistic therapies.

Natl Sci Rev

August 2025

Center for AIE Research, Shenzhen Key Laboratory of Polymer Science and Technology, Guangdong Provincial Key Laboratory of New Energy Materials Service Safety, College of Material Science and Engineering, Shenzhen University, Shenzhen 518060, China.

Multimodal phototheranostics has been recognized as one of the most momentous advances in cancer treatment. Of particular interest is a single molecular species simultaneously featuring in multiple imaging and synergistic phototherapies; the development of such a molecular species is nevertheless a formidably challenging task. Herein, we innovatively designed and synthesized three aggregation-induced emission (AIE)-active molecules with emission in the second near-infrared (NIR-II) window, by employing 10-indeno[1,2-][1,2,5]thiadiazolo[3,4-]quinoxalin-10-one as the electron acceptor, 4-(-butyl)--(4-(-butyl)phenyl)--phenylaniline as the electron donor, and different π-bridge moieties.

View Article and Find Full Text PDF

A thermostable paraoxonase (S3wahi-PON) from sp. strain S3wahi was recently characterised and shown to possess stability across a broad temperature range. This study expands upon the initial biochemical characterisation of S3wahi-PON by investigating the structural determinants and conformational adaptability that contribute to its thermostability, using an integrated approach that combines biophysical techniques and molecular dynamics (MD) simulations across a temperature range of 10 °C to 90 °C.

View Article and Find Full Text PDF

Singlet oxygen (O) plays a crucial role in cancer chemotherapy and ROS biology, driving the need for highly specific probes to monitor its dynamics in real time. Herein, we developed the ratiometric fluorescent probe NAP-t-PY, utilizing a 2-pyridone recognition unit. The probe's 1-methyl-3-benzyl-2-pyridone moiety reacts specifically with O [4 + 2] cycloaddition, forming the endoperoxide NAP-t-PY-EP.

View Article and Find Full Text PDF

Photophysical studies on the interaction of small molecules with various forms of nucleic acids are attracting attention nowadays in order to delineate the molecular level mechanism of various biological processes occurring in vivo. Herein, we employed vivid steady-state and time-resolved spectroscopic techniques to elucidate the detailed characterization of the binding interaction of a biologically active cationic dye thioflavin T (ThT) with double and triple helical forms of RNA - A.U duplex and U.

View Article and Find Full Text PDF