A supramolecular assembly based on an engineered hemoprotein exhibiting a thermal stimulus-driven conversion to a new distinct supramolecular structure

2017 ◽  
Vol 53 (51) ◽  
pp. 6879-6882 ◽  
Author(s):  
Koji Oohora ◽  
Yoshitaka Onuma ◽  
Yuta Tanaka ◽  
Akira Onoda ◽  
Takashi Hayashi

An engineered hemoprotein monomer forms a stable fiber-type assembly and metastable micelle-type assembly induced by transient thermal stimulus.

2021 ◽  
Author(s):  
Saptarshi Chakraborty ◽  
Rajesh Khamrui ◽  
Suhrit Ghosh

Supramolecular structure directing unit regulated co-assembly of a protein produces a highly stable fibrillar nanostructure and glutathione responsive release of the protein in its active state.


2019 ◽  
Vol 21 (36) ◽  
pp. 19879-19889
Author(s):  
María Mar Quesada-Moreno ◽  
Juan Ramón Avilés-Moreno ◽  
Juan Jesús López-González ◽  
Fco. Javier Zúñiga ◽  
Dolores Santa María ◽  
...  

4aα (chiral) and 4aβ (achiral) polymorphs of 1H-benzotriazole are studied by X-ray crystallography, SSNMR, IR, Raman, VCD, and quantum chemical calculations. The absolute configuration of the supramolecular structure of 4aα polymorph is determined.


2015 ◽  
Vol 51 (59) ◽  
pp. 11757-11760 ◽  
Author(s):  
Dawei Xu ◽  
Derek Dustin ◽  
Linhai Jiang ◽  
Damien S. K. Samways ◽  
He Dong

In this work, we will demonstrate the supramolecular assembly of single-chain cationic peptides into stable macromolecular filamentous nanostructures and investigate their supramolecular structure-dependent membrane activity for the development of highly efficient therapeutic carriers.


RSC Advances ◽  
2016 ◽  
Vol 6 (19) ◽  
pp. 15911-15919 ◽  
Author(s):  
Dawei Xu ◽  
Qian Ran ◽  
Yang Xiang ◽  
Linhai Jiang ◽  
Britannia M. Smith ◽  
...  

In this work we will demonstrate the supramolecular assembly of antimicrobial peptides and the effect of PEGylation and nanostructure on biocompatibility with human red blood cells.


2008 ◽  
Vol 63 (7) ◽  
pp. 877-879
Author(s):  
Oscar E. Piro ◽  
Juan Zinczuk ◽  
Enrique J. Baran

The crystal structure of pyridinium thiosaccharinate thiosaccharin, [HNC5H5]+ [(tsac)(Htsac)]− (Htsac = C7H5NO2S2, the thiosaccharin molecule), was determined by single-crystal X-ray diffraction. Both, the thiosaccharinate anion, the corresponding neutral molecule and the pyridinium cation are nearly planar and arranged in the solid state in an almost parallel fashion, hence giving rise to a layered supramolecular structure. The anion shows small but significant modifications in the bonding of the thioamide group as compared with the neutral molecule. The crystal is further stabilized by an extensive H-bonding network. The FTIR spectrum of the compound is briefly commented.


Author(s):  
Asish C. Nag ◽  
Lee D. Peachey

Cat extraocular muscles consist of two regions: orbital, and global. The orbital region contains predominantly small diameter fibers, while the global region contains a variety of fibers of different diameters. The differences in ultrastructural features among these muscle fibers indicate that the extraocular muscles of cats contain at least five structurally distinguishable types of fibers.Superior rectus muscles were studied by light and electron microscopy, mapping the distribution of each fiber type with its distinctive features. A mixture of 4% paraformaldehyde and 4% glutaraldehyde was perfused through the carotid arteries of anesthetized adult cats and applied locally to exposed superior rectus muscles during the perfusion.


Author(s):  
Julia T. Luck ◽  
C. W. Boggs ◽  
S. J. Pennycook

The use of cross-sectional Transmission Electron Microscopy (TEM) has become invaluable for the characterization of the near-surface regions of semiconductors following ion-implantation and/or transient thermal processing. A fast and reliable technique is required which produces a large thin region while preserving the original sample surface. New analytical techniques, particularly the direct imaging of dopant distributions, also require good thickness uniformity. Two methods of ion milling are commonly used, and are compared below. The older method involves milling with a single gun from each side in turn, whereas a newer method uses two guns to mill from both sides simultaneously.


Author(s):  
U. Aebi ◽  
R. Millonig ◽  
H. Salvo

To date, most 3-D reconstructions of undecorated actin filaments have been obtained from actin filament paracrystal data (for refs, see 1,2). However, due to the fact that (a) the paracrystals may be several filament layers thick, and (b) adjacent filaments may sustantially interdigitate, these reconstructions may be subject to significant artifacts. None of these reconstructions has permitted unambiguous tracing or orientation of the actin subunits within the filament. Furthermore, measured values for the maximal filament diameter both determined by EM and by X-ray diffraction analysis, vary between 6 and 10 nm. Obviously, the apparent diameter of the actin filament revealed in the EM will critically depend on specimen preparation, since it is a rather flexible supramolecular assembly which can easily be bent or distorted. To resolve some of these ambiguities, we have explored specimen preparation conditions which may preserve single filaments sufficiently straight and helically ordered to be suitable for single filament 3-D reconstructions, possibly revealing molecular detail.


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