4 research outputs found
Controlled interfacial assembly of 2D curved colloidal crystals and jammed shells
Assembly of colloidal particles on fluid interfaces is a promising technique
for synthesizing two-dimensional micro-crystalline materials useful in fields
as diverse as biomedicine1, materials science2, mineral flotation3 and food
processing4. Current approaches rely on bulk emulsification methods, require
further chemical and thermal treatments, and are restrictive with respect to
the materials employed5-9. The development of methods that exploit the great
potential of interfacial assembly for producing tailored materials have been
hampered by the lack of understanding of the assembly process. Here we report a
microfluidic method that allows direct visualization and understanding of the
dynamics of colloidal crystal growth on curved interfaces. The crystals are
periodically ejected to form stable jammed shells, which we refer to as
colloidal armour. We propose that the energetic barriers to interfacial crystal
growth and organization can be overcome by targeted delivery of colloidal
particles through hydrodynamic flows. Our method allows an unprecedented degree
of control over armour composition, size and stability.Comment: 18 pages, 5 figure
Prediction of Protein Domain with mRMR Feature Selection and Analysis
The domains are the structural and functional units of proteins. With the avalanche of protein sequences generated in the postgenomic age, it is highly desired to develop effective methods for predicting the protein domains according to the sequences information alone, so as to facilitate the structure prediction of proteins and speed up their functional annotation. However, although many efforts have been made in this regard, prediction of protein domains from the sequence information still remains a challenging and elusive problem. Here, a new method was developed by combing the techniques of RF (random forest), mRMR (maximum relevance minimum redundancy), and IFS (incremental feature selection), as well as by incorporating the features of physicochemical and biochemical properties, sequence conservation, residual disorder, secondary structure, and solvent accessibility. The overall success rate achieved by the new method on an independent dataset was around 73%, which was about 28β40% higher than those by the existing method on the same benchmark dataset. Furthermore, it was revealed by an in-depth analysis that the features of evolution, codon diversity, electrostatic charge, and disorder played more important roles than the others in predicting protein domains, quite consistent with experimental observations. It is anticipated that the new method may become a high-throughput tool in annotating protein domains, or may, at the very least, play a complementary role to the existing domain prediction methods, and that the findings about the key features with high impacts to the domain prediction might provide useful insights or clues for further experimental investigations in this area. Finally, it has not escaped our notice that the current approach can also be utilized to study protein signal peptides, B-cell epitopes, HIV protease cleavage sites, among many other important topics in protein science and biomedicine
The actin homologue MreB organizes the bacterial cell membrane
The eukaryotic cortical actin cytoskeleton creates specific lipid domains, including lipid rafts, which determine the distribution of many membrane proteins. Here we show that the bacterial actin homologue MreB displays a comparable activity. MreB forms membrane-associated filaments that coordinate bacterial cell wall synthesis. We noticed that the MreB cytoskeleton influences fluorescent staining of the cytoplasmic membrane. Detailed analyses combining an array of mutants, using specific lipid staining techniques and spectroscopic methods, revealed that MreB filaments create specific membrane regions with increased fluidity (RIFs). Interference with these fluid lipid domains (RIFs) perturbs overall lipid homeostasis and affects membrane protein localization. The influence of MreB on membrane organization and fluidity may explain why the active movement of MreB stimulates membrane protein diffusion. These novel MreB activities add additional complexity to bacterial cell membrane organization and have implications for many membrane-associated processes