Stabilization of backbone‐circularized protein is attained by synergistic gains in enthalpy of folded structure and entropy of unfolded structure

FEBS Journal ◽  
2019 ◽  
Vol 287 (8) ◽  
pp. 1554-1575 ◽  
Author(s):  
Risa Shibuya ◽  
Takamitsu Miyafusa ◽  
Shinya Honda
Keyword(s):  
Folded Structure ◽  
Synergistic Gains

scholarly journals The N-terminal rhodanese domain fromAzotobacter vinelandiihas a stable and folded structure independently of the C-terminal domain

FEBS Letters ◽  
2004 ◽  
Vol 577 (3) ◽  
pp. 403-408 ◽  
Author(s):  
Sonia Melino ◽  
Daniel O. Cicero ◽  
Fabio Forlani ◽  
Silvia Pagani ◽  
Maurizio Paci
Keyword(s):  
Terminal Domain ◽  
Folded Structure

Synergistic gains from the multi-objective optimal operation of cascade reservoirs in the Upper Yellow River basin

2015 ◽  
Vol 523 ◽  
pp. 758-767 ◽  
Author(s):  
Tao Bai ◽  
Jian-xia Chang ◽  
Fi-John Chang ◽  
Qiang Huang ◽  
Yi-min Wang ◽  
...  
Keyword(s):  
River Basin ◽  
Yellow River ◽  
Yellow River Basin ◽  
Optimal Operation ◽  
Cascade Reservoirs ◽  
Multi Objective ◽  
Upper Yellow River ◽  
Synergistic Gains

scholarly journals Multiple Roles of Flagellar Export Chaperones for Efficient and Robust Flagellar Filament Formation in Salmonella

2021 ◽  
Vol 12 ◽  
Author(s):  
Tohru Minamino ◽  
Yusuke V. Morimoto ◽  
Miki Kinoshita ◽  
Keiichi Namba
Keyword(s):  
Type Iii Secretion ◽  
Culture Media ◽  
Multiple Roles ◽  
Filament Formation ◽  
Dynamic Interactions ◽  
Filament Assembly ◽  
Suppressor Mutations ◽  
Folded Structure ◽  
Flagellar Filament

FlgN, FliS, and FliT are flagellar export chaperones specific for FlgK/FlgL, FliC, and FliD, respectively, which are essential component proteins for filament formation. These chaperones facilitate the docking of their cognate substrates to a transmembrane export gate protein, FlhA, to facilitate their subsequent unfolding and export by the flagellar type III secretion system (fT3SS). Dynamic interactions of the chaperones with FlhA are thought to determine the substrate export order. To clarify the role of flagellar chaperones in filament assembly, we constructed cells lacking FlgN, FliS, and/or FliT. Removal of either FlgN, FliS, or FliT resulted in leakage of a large amount of unassembled FliC monomers into the culture media, indicating that these chaperones contribute to robust and efficient filament formation. The ∆flgN ∆fliS ∆fliT (∆NST) cells produced short filaments similarly to the ∆fliS mutant. Suppressor mutations of the ∆NST cells, which lengthened the filament, were all found in FliC and destabilized the folded structure of FliC monomer. Deletion of FliS inhibited FliC export and filament elongation only after FliC synthesis was complete. We propose that FliS is not involved in the transport of FliC upon onset of filament formation, but FliS-assisted unfolding of FliC by the fT3SS becomes essential for its rapid and efficient export to form a long filament when FliC becomes fully expressed in the cytoplasm.

scholarly journals Получение нерастворимых в воде пленок из фиброина шелка, исследование их структуры и свойств

2021 ◽  
Vol 91 (12) ◽  
pp. 2080
Author(s):  
Ю.А. Нащекина ◽  
В.С. Коныгина ◽  
Е.Н. Попова ◽  
В.В. Кодолова-Чухонцева ◽  
А.В. Нащекин ◽  
...  
Keyword(s):  
Silk Fibroin ◽  
Structural Transition ◽  
Conformational Transition ◽  
Cell Cultivation ◽  
Natural Polymers ◽  
Suture Materials ◽  
Scanning Calorimetry ◽  
Disordered Structure ◽  
Folded Structure ◽  
Scope Of Application

Silk fibroin is one of the promising natural polymers that already being used in medicine to forming of suture materials. The possibility of forming scaffolds in the form of films, sponges or gels for cell cultivation and transplantation will significantly expand the scope of application of this material in tissue engineering. The conditions for obtaining silk fibroin insoluble in water in the form of films were worked out. The structural transition on the surface of the films to a coarsely fragmented state after treatment of the films with methanol was demonstrated using optical microscopy. Using FTIR spectroscopy, the conformational transition of silk fibroin from the disordered structure of the untreated film to the β-folded structure was confirmed. Using the method of differential scanning calorimetry, the glass transition temperature of the native film was determined as 216 °C. The study of the mechanical properties of silk fibroin films in a liquid medium showed that their strength decreases and their elasticity increases by almost 15 times compared to tests of the same films in a dry state.

scholarly journals Optimised production of disulfide-bonded fungal effectors in E. coli using CyDisCo and FunCyDisCo co-expression approaches

2021 ◽  
Author(s):  
Daniel Yu ◽  
Megan A Outram ◽  
Emma Creen ◽  
Ashley Smith ◽  
Yi-Chang Sung ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Disulfide Bonds ◽  
Fungal Pathogens ◽  
Sequence Similarity ◽  
Expression System ◽  
Pathogenic Fungi ◽  
Efficient Production ◽  
E Coli ◽  
Functional Studies ◽  
Folded Structure

Effectors are a key part of the arsenal of plant pathogenic fungi and promote pathogen virulence and disease. Effectors typically lack sequence similarity to proteins with known functional domains and motifs, limiting our ability to predict their functions and understand how they are recognised by plant hosts. As a result, cross-disciplinary approaches involving structural biology and protein biochemistry are often required to decipher and better characterise effector function. These approaches are reliant on high yields of relatively pure protein, which often requires protein production using a heterologous expression system. For some effectors, establishing an efficient production system can be difficult, particularly those that require multiple disulfide bonds to achieve their naturally folded structure. Here, we describe the use of a co-expression system within the heterologous host E. coli termed CyDisCo (cytoplasmic disulfide bond formation in E. coli) to produce disulfide bonded fungal effectors. We demonstrate that CyDisCo and a naturalised co-expression approach termed FunCyDisCo (Fungi-CyDisCo) can significantly improve the production yields of numerous disulfide bonded effectors from diverse fungal pathogens. The ability to produce large quantities of functional recombinant protein has facilitated functional studies and crystallisation of several of these reported fungal effectors. We suggest this approach could be broadly useful in the investigation of the function and recognition of a broad range of disulfide-bond containing effectors.

scholarly journals Optical Design for a Head-Mounted Display

1993 ◽  
Vol 2 (3) ◽  
pp. 185-202 ◽  
Author(s):  
Jiantao Ma ◽  
John M. Hollerbach ◽  
Ian W. Hunter
Keyword(s):  
Optical Design ◽  
Field Of View ◽  
Wide Field ◽  
Optical System Design ◽  
Head Mounted Display ◽  
Cost Constraints ◽  
Field Curvature ◽  
Folded Structure ◽  
Wide Field Of View ◽  
Color Field

This paper presents a design concept for a head-mounted display, incorporating color stereo vision using commercial LCDs and our own optical relay design. The focus here is on the optical system design, which must meet specifications for a wide field of view, size and cost constraints, and aberration minimization based on human factors. Two multispherical lens systems are presented and compared, one a straight structure and the other a folded structure, which satisfy the design constraints. Their aberrations (distortion, coma, lateral color, field curvature, and astigmatism) have been well corrected, according to human perceptual constraints explicitly discussed. Each has a 20-mm eye relief and an instantaneous field of view greater than 60°; the former has an exit pupil of 10 mm and the latter of 8 mm.

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