Gotowe bibliografie tematyczne / Protein Conformation - Air/Water Interface

Spis treści

Artykuły w czasopismach

Gotowa bibliografia na temat „Protein Conformation - Air/Water Interface”

Autor: Grafiati

Data publikacji: 7 września 2023

Utwórz poprawne odniesienie w stylach APA, MLA, Chicago, Harvard i wielu innych

Wybierz rodzaj źródła:

Zobacz listy aktualnych artykułów, książek, rozpraw, streszczeń i innych źródeł naukowych na temat „Protein Conformation - Air/Water Interface”.

Przycisk „Dodaj do bibliografii” jest dostępny obok każdej pracy w bibliografii. Użyj go – a my automatycznie utworzymy odniesienie bibliograficzne do wybranej pracy w stylu cytowania, którego potrzebujesz: APA, MLA, Harvard, Chicago, Vancouver itp.

Możesz również pobrać pełny tekst publikacji naukowej w formacie „.pdf” i przeczytać adnotację do pracy online, jeśli odpowiednie parametry są dostępne w metadanych.

Artykuły w czasopismach na temat "Protein Conformation - Air/Water Interface"

Han, Fei, Qian Shen, Wei Zheng, et al. "The Conformational Changes of Bovine Serum Albumin at the Air/Water Interface: HDX-MS and Interfacial Rheology Analysis." Foods 12, no. 8 (2023): 1601. http://dx.doi.org/10.3390/foods12081601.

Pełny tekst źródła

Streszczenie:

The characterization and dynamics of protein structures upon adsorption at the air/water interface are important for understanding the mechanism of the foamability of proteins. Hydrogen–deuterium exchange, coupled with mass spectrometry (HDX-MS), is an advantageous technique for providing conformational information for proteins. In this work, an air/water interface, HDX-MS, for the adsorbed proteins at the interface was developed. The model protein bovine serum albumin (BSA) was deuterium-labeled at the air/water interface in situ for different predetermined times (10 min and 4 h), and then the resulting mass shifts were analyzed by MS. The results indicated that peptides 54–63, 227–236, and 355–366 of BSA might be involved in the adsorption to the air/water interface. Moreover, the residues L55, H63, R232, A233, L234, K235, A236, R359, and V366 of these peptides might interact with the air/water interface through hydrophobic and electrostatic interactions. Meanwhile, the results showed that conformational changes of peptides 54–63, 227–236, and 355–366 could lead to structural changes in their surrounding peptides, 204–208 and 349–354, which could cause the reduction of the content of helical structures in the rearrangement process of interfacial proteins. Therefore, our air/water interface HDX-MS method could provide new and meaningful insights into the spatial conformational changes of proteins at the air/water interface, which could help us to further understand the mechanism of protein foaming properties.

Style APA, Harvard, Vancouver, ISO itp.

Yano, Yohko F., Etsuo Arakawa, Wolfgang Voegeli, Chika Kamezawa, and Tadashi Matsushita. "Initial Conformation of Adsorbed Proteins at an Air–Water Interface." Journal of Physical Chemistry B 122, no. 17 (2018): 4662–66. http://dx.doi.org/10.1021/acs.jpcb.8b01039.

Pełny tekst źródła

Style APA, Harvard, Vancouver, ISO itp.

Lad, Mitaben D., Fabrice Birembaut, Joanna M. Matthew, Richard A. Frazier, and Rebecca J. Green. "The adsorbed conformation of globular proteins at the air/water interface." Physical Chemistry Chemical Physics 8, no. 18 (2006): 2179. http://dx.doi.org/10.1039/b515934b.

Pełny tekst źródła

Style APA, Harvard, Vancouver, ISO itp.

Belem-Gonçalves, Silvia, Pascale Tsan, Jean-Marc Lancelin, Tito L. M. Alves, Vera M. Salim, and Françoise Besson. "Interfacial behaviour of bovine testis hyaluronidase." Biochemical Journal 398, no. 3 (2006): 569–76. http://dx.doi.org/10.1042/bj20060485.

Pełny tekst źródła

Streszczenie:

The interfacial properties of bovine testicular hyaluronidase were investigated by demonstrating the association of hyaluronidase activity with membranes prepared from bovine testis. Protein adsorption to the air/water interface was investigated using surface pressure-area isotherms. In whichever way the interfacial films were obtained (protein injection or deposition), the hyaluronidase exhibited a significant affinity for the air/water interface. The isotherm obtained 180 min after protein injection into a pH 5.3 subphase was similar to the isotherm obtained after spreading the same amount of protein onto the same subphase, indicating that bovine testicular hyaluronidase molecules adopted a similar arrangement and/or conformation at the interface. Increasing the subphase pH from 5.3 to 8 resulted in changes of the protein isotherms. These modifications, which could correspond to the small pH-induced conformational changes observed by Fourier-transform IR spectroscopy, were discussed in relation to the pH influence on the hyaluronidase activity. Adding hyaluronic acid, the enzyme substrate, to the subphase tested the stability of the interfacial properties of hyaluronidase. The presence of hyaluronic acid in the subphase did not modify the protein adsorption and allowed substrate binding to a preformed film of hyaluronidase at pH 5.3, the optimal pH for the enzyme activity. Such effects of hyaluronic acid were not observed when the subphase was constituted of pure water, a medium where the enzyme activity was negligible. These influences of hyaluronic acid were discussed in relation to the modelled structure of bovine testis hyaluronidase where a hydrophobic region was proposed to be opposite of the catalytic site.

Style APA, Harvard, Vancouver, ISO itp.

Bhuvanesh, Thanga, Rainhard Machatschek, Yue Liu, Nan Ma, and Andreas Lendlein. "Self-stabilized fibronectin films at the air/water interface." MRS Advances 5, no. 12-13 (2019): 609–20. http://dx.doi.org/10.1557/adv.2019.401.

Pełny tekst źródła

Streszczenie:

ABSTRACTFibronectin (FN) is a mediator molecule, which can connect cell receptors to the extracellular matrix (ECM) in tissues. This function is highly desirable for biomaterial surfaces in order to support cell adhesion. Controlling the fibronectin adsorption profile on substrates is challenging because of possible conformational changes after deposition, or due to displacement by secondary proteins from the culture medium. Here, we aim to develop a method to realize self-stabilized ECM glycoprotein layers with preserved native secondary structure on substrates. Our concept is the assembly of FN layers at the air-water (A-W) interface by spreading FN solution as droplets on the interface and transfer of the layer by the Langmuir-Schäfer (LS) method onto a substrate. It is hypothesized that 2D confinement and high local concentration at A-W interface supports FN self-interlinking to form cohesive films. Rising surface pressure with time, plateauing at 10.5 mN·m-1 (after 10 hrs), indicated that FN was self-assembling at the A-W interface. In situ polarization-modulation infrared reflection absorption spectroscopy of the layer revealed that FN maintained its native anti-parallel β-sheet structure after adsorption at the A-W interface. FN self-interlinking and elasticity was shown by the increase in elastic modulus and loss modulus with time using interfacial rheology. A network-like structure of FN films formed at the A-W interface was confirmed by atomic force microscopy after LS transfer onto Si-wafer. FN films consisted of native, globular FN molecules self-stabilized by intermolecular interactions at the A-W interface. Therefore, the facile FN self-stabilized network-like films with native anti-parallel β-sheet structure produced here, could serve as stable ECM protein coatings to enhance cell attachment on in vitro cell culture substrates and planar implant materials.

Style APA, Harvard, Vancouver, ISO itp.

Guo, Dashan, Yuwei Hou, Hongshan Liang, Lingyu Han, Bin Li, and Bin Zhou. "Mechanism of Reduced Glutathione Induced Lysozyme Defolding and Molecular Self-Assembly." Foods 12, no. 10 (2023): 1931. http://dx.doi.org/10.3390/foods12101931.

Pełny tekst źródła

Streszczenie:

The distinctive assembly behaviors of lysozyme (Lys) feature prominently in food, materials, biomedicine, and other fields and have intrigued many scholars. Although our previous work suggested that reduced glutathione (GSH) could induce lysozyme to form interfacial films at the air/water interface, the underlying mechanism is still obscure. In the present study, the effects of GSH on the disulfide bond and protein conformation of lysozyme were investigated by fluorescence spectroscopy, circular dichroism spectroscopy, and infrared spectroscopy. The findings demonstrated that GSH was able to break the disulfide bond in lysozyme molecules through the sulfhydryl/disulfide bond exchange reaction, thereby unraveling the lysozyme. The β-sheet structure of lysozyme expanded significantly, while the contents of α-helix and β-turn decreased. Furthermore, the interfacial tension and morphology analysis supported that the unfolded lysozyme tended to arrange macroscopic interfacial films at the air/water interface. It was found that pH and GSH concentrations had an impact on the aforementioned processes, with higher pH or GSH levels having a positive effect. This paper on the exploration of the mechanism of GSH-induced lysozyme interface assembly and the development of lysozyme-based green coatings has better instructive significance.

Style APA, Harvard, Vancouver, ISO itp.

Renault, Anne, Jean-François Rioux-Dubé, Thierry Lefèvre, et al. "Surface Properties and Conformation of Nephila clavipes Spider Recombinant Silk Proteins at the Air−Water Interface." Langmuir 25, no. 14 (2009): 8170–80. http://dx.doi.org/10.1021/la900475q.

Pełny tekst źródła

Style APA, Harvard, Vancouver, ISO itp.

Han, Meng-huai, and Chi-cheng Chiu. "Fast estimation of protein conformational preference at air/water interface via molecular dynamics simulations." Journal of the Taiwan Institute of Chemical Engineers 92 (November 2018): 42–49. http://dx.doi.org/10.1016/j.jtice.2018.02.026.

Pełny tekst źródła

Style APA, Harvard, Vancouver, ISO itp.

Flach, Carol R., Joseph W. Brauner, and Richard Mendelsohn. "Coupled External Reflectance FT-IR/Miniaturized Surface Film Apparatus for Biophysical Studies." Applied Spectroscopy 47, no. 7 (1993): 982–85. http://dx.doi.org/10.1366/0003702934415147.

Pełny tekst źródła

Streszczenie:

An FT-IR spectrophotometer has been interfaced to a miniaturized surface film apparatus for external reflection studies of insoluble monolayers in situ at the air/water interface. Signal-to-noise ratios of 200:1 were routinely achieved for the CH2 stretching vibrations of phospholipids. We have monitored, using the acyl chain symmetric CH2 stretching frequency near 2850 cm−1 as a structural probe, lipid conformational order changes that occur during the surface pressure-induced two-dimensional phase transition in monolayers of 1,2-dipalmitoylphosphatidylserine. In addition, the small volume of the miniaturized film apparatus (30 mL) permitted replacement of H2O with D2O in the subphase. This capability, in turn, permits the acquisition of spectral data in the amide I region of proteins. We report the first external reflection FT-IR spectrum of an insoluble protein monolayer. The protein studied is pulmonary surfactant SP-C.

Style APA, Harvard, Vancouver, ISO itp.

Tanaka, Takumi, Yuki Terauchi, Akira Yoshimi, and Keietsu Abe. "Aspergillus Hydrophobins: Physicochemical Properties, Biochemical Properties, and Functions in Solid Polymer Degradation." Microorganisms 10, no. 8 (2022): 1498. http://dx.doi.org/10.3390/microorganisms10081498.

Pełny tekst źródła

Streszczenie:

Hydrophobins are small amphipathic proteins conserved in filamentous fungi. In this review, the properties and functions of Aspergillus hydrophobins are comprehensively discussed on the basis of recent findings. Multiple Aspergillus hydrophobins have been identified and categorized in conventional class I and two non-conventional classes. Some Aspergillus hydrophobins can be purified in a water phase without organic solvents. Class I hydrophobins of Aspergilli self-assemble to form amphipathic membranes. At the air–liquid interface, RolA of Aspergillus oryzae self-assembles via four stages, and its self-assembled films consist of two layers, a rodlet membrane facing air and rod-like structures facing liquid. The self-assembly depends mainly on hydrophobin conformation and solution pH. Cys4–Cys5 and Cys7–Cys8 loops, disulfide bonds, and conserved Cys residues of RodA-like hydrophobins are necessary for self-assembly at the interface and for adsorption to solid surfaces. AfRodA helps Aspergillus fumigatus to evade recognition by the host immune system. RodA-like hydrophobins recruit cutinases to promote the hydrolysis of aliphatic polyesters. This mechanism appears to be conserved in Aspergillus and other filamentous fungi, and may be beneficial for their growth. Aspergilli produce various small secreted proteins (SSPs) including hydrophobins, hydrophobic surface–binding proteins, and effector proteins. Aspergilli may use a wide variety of SSPs to decompose solid polymers.

Style APA, Harvard, Vancouver, ISO itp.

Więcej źródeł

Oferujemy zniżki na wszystkie plany premium dla autorów, których prace zostały uwzględnione w tematycznych zestawieniach literatury. Skontaktuj się z nami, aby uzyskać unikalny kod promocyjny!