Spin polarized 3He: From basic research to medical applications

2013 ◽  
Vol 44 (6) ◽  
pp. 904-908 ◽  
Author(s):  
S. Karpuk ◽  
F. Allmendinger ◽  
M. Burghoff ◽  
C. Gemmel ◽  
M. Güldner ◽  
...  
1996 ◽  
Vol 74 (2) ◽  
pp. 133-154 ◽  
Author(s):  
Robert S. Hodges

The two-stranded α-helical coiled-coil is a universal dimerization domain used by nature in a diverse group of proteins. The simplicity of the coiled-coil structure makes it an ideal model system to use in understanding the fundamentals of protein folding and stability and in testing the principles of de novo design. The issues that must be addressed in the de novo design of coiled-coils for use in research and medical applications are (i) controlling parallel versus antiparallel orientation of the polypeptide chains, (ii) controlling the number of helical strands in the assembly (iii) maximizing stability of homodimers or heterodimers in the shortest possible chain length that may require the engineering of covalent constraints, and (iv) the ability to have selective heterodimerization without homodimerization, which requires a balancing of selectivity versus affinity of the dimerization strands. Examples of our initial inroads in using this de novo design motif in various applications include: heterodimer technology for the detection and purification of recombinant peptides and proteins; a universal dimerization domain for biosensors; a two-stage targeting and delivery system; and coiled-coils as templates for combinatorial helical libraries for basic research and drug discovery and as synthetic carrier molecules. The universality of this dimerization motif in nature suggests an endless number of possibilities for its use in de novo design, limited only by the creativity of peptide–protein engineers.Key words: de novo design of proteins, α-helical coiled-coils, protein folding, protein stability, dimerization domain, dimerization motif.


2013 ◽  
Vol 2013 ◽  
pp. 1-16 ◽  
Author(s):  
Céline Huynen ◽  
Patrice Filée ◽  
André Matagne ◽  
Moreno Galleni ◽  
Mireille Dumoulin

Designing hybrid proteins is a major aspect of protein engineering and covers a very wide range of applications from basic research to medical applications. This review focuses on the use of class Aβ-lactamases as versatile scaffolds to design hybrid enzymes (referred to asβ-lactamase hybrid proteins, BHPs) in which an exogenous peptide, protein or fragment thereof is inserted at various permissive positions. We discuss how BHPs can be specifically designed to create bifunctional proteins, to produce and to characterize proteins that are otherwise difficult to express, to determine the epitope of specific antibodies, to generate antibodies against nonimmunogenic epitopes, and to better understand the structure/function relationship of proteins.


Polymers ◽  
2021 ◽  
Vol 13 (20) ◽  
pp. 3572
Author(s):  
Andrzej S. Swinarew ◽  
Beata Swinarew ◽  
Tomasz Flak ◽  
Hubert Okła ◽  
Marta Lenartowicz-Klik ◽  
...  

This research aimed to examine the mechanical properties of polycarbonate-based composites filled with both organic and inorganic reinforcements before and after simulated environmental degradation. Series of polycarbonate-based samples were prepared in the form of thin tapes. Their rheological properties were examined. Then, the samples were exposed to artificial environmental conditions. Finally, their rheological properties were examined once more, and the results were compared with those obtained for untreated samples. This paper presents basic research on the application of inorganic fillers to polycarbonate in order to determine the influence of the filler on the behavior of the obtained material. The aim of the work was to determine the usefulness and purpose of using this type of filler in polycarbonates for applications in contact with ultraviolet radiation, especially medical applications.


Author(s):  
Xinjie Chen ◽  
Yuan Lu

Circular RNA (circRNA) is a unique type of noncoding RNA molecule. Compared with traditional linear RNA, circRNA is a covalently closed circle produced by a process called backsplicing. CircRNA is abundant in many cells and has rich functions in cells, such as acting as miRNA sponge, protein sponge, protein scaffold, and mRNA regulator. With the continuous development of circRNA study, circRNA has also played an important role in medical applications, including circRNA vaccines and gene therapy. In this review, we illustrate the synthesis of circRNAs in vitro. We focus on biological ligation methods, such as enzymatic ligation from the bacteriophage T4 and ribozyme method. In addition, we summarize the current challenges in the design, synthesis, application, and production of circRNAs, and propose possible solutions in the future. CircRNA is expected to play an essential role in basic research and medical applications.


Author(s):  
M. Nishigaki ◽  
S. Katagiri ◽  
H. Kimura ◽  
B. Tadano

The high voltage electron microscope has many advantageous features in comparison with the ordinary electron microscope. They are a higher penetrating efficiency of the electron, low chromatic aberration, high accuracy of the selected area diffraction and so on. Thus, the high voltage electron microscope becomes an indispensable instrument for the metallurgical, polymer and biological specimen studies. The application of the instrument involves today not only basic research but routine survey in the various fields. Particularly for the latter purpose, the performance, maintenance and reliability of the microscope should be same as those of commercial ones. The authors completed a 500 kV electron microscope in 1964 and a 1,000 kV one in 1966 taking these points into consideration. The construction of our 1,000 kV electron microscope is described below.


Author(s):  
M.J. Hennessy ◽  
E. Kwok

Much progress in nuclear magnetic resonance microscope has been made in the last few years as a result of improved instrumentation and techniques being made available through basic research in magnetic resonance imaging (MRI) technologies for medicine. Nuclear magnetic resonance (NMR) was first observed in the hydrogen nucleus in water by Bloch, Purcell and Pound over 40 years ago. Today, in medicine, virtually all commercial MRI scans are made of water bound in tissue. This is also true for NMR microscopy, which has focussed mainly on biological applications. The reason water is the favored molecule for NMR is because water is,the most abundant molecule in biology. It is also the most NMR sensitive having the largest nuclear magnetic moment and having reasonable room temperature relaxation times (from 10 ms to 3 sec). The contrast seen in magnetic resonance images is due mostly to distribution of water relaxation times in sample which are extremely sensitive to the local environment.


Author(s):  
Kazuyuki Koike ◽  
Hideo Matsuyama

Spin-polarized scanning electron microscopy (spin SEM), where the secondary electron spin polarization is used as the image signal, is a novel technique for magnetic domain observation. Since its first development by Koike and Hayakawa in 1984, several laboratories have extensively studied this technique and have greatly improved its capability for data extraction and its range of applications. This paper reviews the progress over the last few years.Almost all the high expectations initially held for spin SEM have been realized. A spatial resolution of several hundreds angstroms has been attained, which is nearly one order of magnitude higher than that of conventional methods for thick samples. Quantitative analysis of magnetization direction has been performed more easily than with conventional methods. Domain observation of the surface of three-dimensional samples has been confirmed to be possible. One of the drawbacks, a long image acquisition time, has been eased by combining highspeed image-signal processing with high speed scanning, although at the cost of image quality. By using spin SEM, the magnetic structure of a 180 degrees surface Neel wall, magnetic thin films, multilayered films, magnetic discs, etc., have been investigated.


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