The handedness of nanometrical helices based on surfactant assemblies was inverted when these helices were in contact with an excess solution of chiral anions with opposite enantiomers. An important difference in the kinetics of chirality inversion at the molecular level and mesoscopic level was observed.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1039/c4cc07972h | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Nucleocapsid assembly drives Ebola viral factory maturation and dispersion.
Cell
December 2024
Schaller Research Groups, Department of Infectious Diseases, Virology, Heidelberg University, Heidelberg, Germany; BioQuant, Heidelberg University, Heidelberg, Germany. Electronic address:
Article Synopsis
- Viral factories (VFs) are membrane-less organelles where negative-sense RNA viruses, like Ebola, replicate and encapsidate their genomes.
- Using advanced imaging techniques, researchers observed how viral nucleocapsids (NCs) change from loose formations to compact structures during the infection process.
- The study found that as VFs mature, they become less spherical and more integrated with cellular components, which likely aids in the transportation of NCs for virus budding.
Mapping the local ambidextrous chirality in thin films of N phase by circular dichroism spectra.
Spectrochim Acta A Mol Biomol Spectrosc
December 2024
Department of Chemistry, University of Hull, Hull HU6 7RX, UK. Electronic address:
Circular dichroism mapping (CDM) method was introduced by utilizing the highly collimated light beam of synchrotron radiation (SR) available at Diamond Light Source B23 beamline for scanning the thin films of the N phase. We apply SR-CDM to two achiral dimeric materials exhibiting the N phase: symmetric DTC5C9 and dissymmetric DTC5C9CB. The SR-CDM measurements directly capture the chiral information in the local N domains, providing the ultimate complement to the theoretical predictions of the helical structures: the spontaneous symmetry breaking in N phase is ambidextrous.
View Article and Find Full Text PDFCircularly Polarized Luminescence in Cellulose-Based Assemblies: Synthesis, Regulation, and Application.
Small
December 2024
State Key Laboratory of Chemical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin, 300072, China.
Currently, circularly polarized luminescence (CPL) has drawn wide interest in 3D display, information storage, and optical sensing. However, traditional synthetic paths are often accompanied by low chiral optical intensity and complex processes. Cellulose nanocrystals (CNCs), with the properties of liquid crystals, can spontaneously arrange into the left-handed layered nanofilm, which enables them candidates in the construction of CPL materials.
View Article and Find Full Text PDFQuaternary arrangements of membrane proteins: an aquaporin case.
Biochem Soc Trans
December 2024
School of Agriculture, Food and Wine, and Waite Research Institute, Faculty of Sciences, Engineering and Technology, University of Adelaide, Glen Osmond, South Australia 5064, Australia.
Integral polytopic α-helical membrane transporters and aquaporins move and distribute various molecules and dispose of or compartmentalize harmful elements that gather in living cells. The view shaped nearly 25 years ago states that integrating these proteins into cellular membranes can be considered a two-stage process, with hydrophobic core folding into α-helices across membranes to form functional entities (Popot and Engelman, 1990; Biochemistry29, 4031-4037). Since then, a large body of evidence cemented the roles of structural properties of membrane proteins and bilayer solvent components in forming functional assemblies.
View Article and Find Full Text PDFProtein-Protein Interaction and Conformational Change in the Alpha-Helical Membrane Transporter BtuCD-F in the Native Cellular Envelope.
Chembiochem
January 2025
Department of Physics, Freie Universität Berlin, Arnimallee 14, Berlin, 14195, Germany.
Alpha-helical membrane proteins perform numerous critical functions essential for the survival of living organisms. Traditionally, these proteins are extracted from membranes using detergent solubilization and reconstitution into liposomes or nanodiscs. However, these processes often obscure the effects of nanoconfinement and the native environment on the structure and conformational heterogeneity of the target protein.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!