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1.
Materials (Basel) ; 16(19)2023 Sep 22.
Article in English | MEDLINE | ID: mdl-37834489

ABSTRACT

Aerospace vehicle connection constructions are in urgent need of joint structures with excellent aerodynamic profiles and environmental adaptability. To address issues such as poor aerodynamic profile, material thermal expansion coefficient mismatch, and limited joint structure evaluation indexes, a multi-bolt, countersunk C/SiC composite joint structure is presented in this study. The development of a 3D Hashin progressive damage model and its dedicated solver code is presented. The validity of the model is confirmed by comparing simulation results with experimental data. Three evaluation indexes are proposed, peak load, weight increment efficiency, and bolt load distribution, to thoroughly evaluate the mechanical performance of multi-bolt, countersunk C/SiC composite joint structures. Using the proposed model and evaluation indices, we evaluate sixteen different designs of multi-bolt, countersunk C/SiC composite joint structures and analyze how design parameters affect their mechanical properties and damage patterns. The results show that the best mechanical properties of the joint structure are achieved when the ratio of bolt pitch to through hole diameter is 3, the ratio of bolt spacing between columns to through hole diameter is 4, the ratio of the distance between the free edge of the substrate to through hole diameter is 1.5, the ratio of through hole diameter to specimen thickness is 1.7, and the ratio of the distance between the edge of the substrate to through hole diameter is 1.5.

2.
Eur Phys J E Soft Matter ; 45(10): 87, 2022 Oct 29.
Article in English | MEDLINE | ID: mdl-36308633

ABSTRACT

A general population model with Allee effect driven by correlated additive and multiplicative white noises is considered. This paper aims to investigate noise-induced phenomenological bifurcation (P-bifurcation) and the influence of noises on the population model. With the help of Fokker-Planck equation, we obtain the stationary probability distribution (SPD) of the model, and find that the shape of SPD experiences a transition from one structure to another when the noise intensity passes through a critical value, i.e., the P-bifurcation occurs. Moreover, detailed analysis and simulations for stochastic logistic-like models with weak and strong Allee effects show that the correlated noises have complex effects on the eventual distribution of population size. This paper aims to investigate noise-induced phenomenological bifurcation (P-bifurcation) for a general population model with Allee effect driven by correlated additive and multiplicative white noises. We find that the shape of SPD experiences a transition from one structure to another when the noise intensity passes through a critical value, i.e., the P-bifurcation occurs.


Subject(s)
Stochastic Processes , Humans
3.
JASA Express Lett ; 1(1): 015205, 2021 Jan.
Article in English | MEDLINE | ID: mdl-36154097

ABSTRACT

Representation learning is believed to produce high-level representations of underlying dynamics in temporal sequences. A three-dimensional convolutional neural network trained to predict future frames in ultrasound tongue and optical lip images creates features for a continuous hidden Markov model based speech recognition system. Predictive tongue features are found to generate lower word error rates than those obtained from an auto-encoder without future frames, or from discrete cosine transforms. Improvement is apparent for the monophone/triphone Gaussian mixture model and deep neural network acoustic models. When tongue and lip modalities are combined, the advantage of the predictive features is reduced.

4.
J Biol Chem ; 293(16): 6075-6089, 2018 04 20.
Article in English | MEDLINE | ID: mdl-29491141

ABSTRACT

Zinc is an essential metal in bacteria. One important bacterial zinc transporter is AdcA, and most bacteria possess AdcA homologs that are single-domain small proteins due to better efficiency of protein biogenesis. However, a double-domain AdcA with two zinc-binding sites is significantly overrepresented in Streptococcus species, many of which are major human pathogens. Using molecular simulation and experimental validations of AdcA from Streptococcus pyogenes, we found here that the two AdcA domains sequentially stabilize the structure upon zinc binding, indicating an organization required for both increased zinc affinity and transfer speed. This structural organization appears to endow Streptococcus species with distinct advantages in zinc-depleted environments, which would not be achieved by each single AdcA domain alone. This enhanced zinc transport mechanism sheds light on the significance of the evolution of the AdcA domain fusion, provides new insights into double-domain transporter proteins with two binding sites for the same ion, and indicates a potential target of antimicrobial drugs against pathogenic Streptococcus species.


Subject(s)
ATP-Binding Cassette Transporters/metabolism , Bacterial Proteins/metabolism , Streptococcus pyogenes/metabolism , Zinc/metabolism , ATP-Binding Cassette Transporters/chemistry , ATP-Binding Cassette Transporters/genetics , Bacterial Proteins/chemistry , Bacterial Proteins/genetics , Binding Sites , Crystallography, X-Ray , Humans , Models, Molecular , Phylogeny , Protein Binding , Protein Conformation , Protein Domains , Streptococcal Infections/microbiology , Streptococcus pyogenes/chemistry , Streptococcus pyogenes/genetics
5.
Sheng Wu Gong Cheng Xue Bao ; 30(1): 76-82, 2014 Jan.
Article in Chinese | MEDLINE | ID: mdl-24818481

ABSTRACT

Gluconobacter oxydans is known to oxidize glucose to gluconic acid (GA), and subsequently, to 2-keto-gluconic acid (2KGA) and 5-keto-gluconic acid (5KGA), while 5KGA can be converted to L-(+)-tartaric acid. In order to increase the production of 5KGA, Gluconobacter oxydans HGI-1 that converts GA to 5KGA exclusively was chosen in this study, and effects of carbon sources (lactose, maltose, sucrose, amylum and glucose) and nitrogen sources (yeast extract, fish meal, corn steep liquor, soybean meal and cotton-seed meal) on 5KGA production were investigated. Results of experiment in 500 mL shake-flask show that the highest yield of 5KGA (98.20 g/L) was obtained using 100 g/L glucose as carbon source. 5KGA reached 100.20 g/L, 109.10 g/L, 99.83 g/L with yeast extract, fish meal and corn steep liquor as nitrogen source respectively, among which the optimal nitrogen source was fish meal. The yield of 5KGA by corn steep liquor is slightly lower than that by yeast extract. For the economic reason, corn steep liquor was selected as nitrogen source and scaled up to 5 L stirred-tank fermentor, and the final concentration of 5KGA reached 93.80 g/L, with its maximum volumetric productivity of 3.48 g/(L x h) and average volumetric productivity of 1.56 g/(L x h). The result obtained in this study showed that carbon and nitrogen sourses for large-scale production of 5KGA by Gluconobacter oxydans HGI-1 were glucose and corn steep liquor, respectively, and the available glucose almost completely (85.93%) into 5KGA.


Subject(s)
Carbon/chemistry , Culture Media/chemistry , Gluconates/metabolism , Gluconobacter oxydans/metabolism , Nitrogen/chemistry , Bioreactors , Fermentation , Industrial Microbiology
6.
Luminescence ; 29(5): 471-9, 2014 Aug.
Article in English | MEDLINE | ID: mdl-24039032

ABSTRACT

The interaction between vincamine (VCM) and human serum albumin (HSA) has been studied using a fluorescence quenching technique in combination with UV/vis absorption spectroscopy, Fourier transform infrared (FT-IR) spectroscopy, circular dichroism (CD) spectroscopy and molecular modeling under conditions similar to human physiological conditions. VCM effectively quenched the intrinsic fluorescence of HSA via static quenching. The binding constants were calculated from the fluorescence data. Thermodynamic analysis by Van't Hoff equation revealed enthalpy change (ΔH) and entropy change (ΔS) were -4.57 kJ/mol and 76.26 J/mol/K, respectively, which indicated that the binding process was spontaneous and the hydrophobic interaction was the predominant force. The distance r between the donor (HSA) and acceptor (VCM) was obtained according to the Förster's theory of non-radiative energy transfer and found to be 4.41 nm. Metal ions, viz., Na(+), K(+), Li(+), Ni(2+), Ca(2+), Zn(2+) and Al(3+) were found to influence binding of the drug to protein. The 3D fluorescence, FT-IR and CD spectral results revealed changes in the secondary structure of the protein upon interaction with VCM. Furthermore, molecular modeling indicated that VCM could bind to the subdomain IIA (site I) of HSA.


Subject(s)
Serum Albumin/chemistry , Spectrum Analysis/methods , Vincamine/chemistry , Binding Sites , Fluorescence , Humans , Hydrophobic and Hydrophilic Interactions , Protein Binding , Thermodynamics
7.
PLoS One ; 8(6): e65682, 2013.
Article in English | MEDLINE | ID: mdl-23840354

ABSTRACT

Lipoprotein FtsB is a component of the FtsABCD transporter that is responsible for ferrichrome binding and uptake in the Gram-positive pathogen Streptococcus pyogenes. In the present study, FtsB was cloned and purified from the bacteria and its Fch binding characteristics were investigated in detail by using various biophysical and biochemical methods. Based on the crystal structures of homogeneous proteins, FtsB was simulated to have bi-lobal structure forming a deep cleft with four residues in the cleft as potential ligands for Fch binding. With the assistance of site-directed mutagenesis, residue Trp204 was confirmed as a key ligand and Tyr137 was identified to be another essential residue for Fch binding. Kinetics experiments demonstrated that Fch binding in FtsB occurred in two steps, corresponding to the bindings to Tyr137 at N-lobe and Trp204 from C-lobe, respectively, and so that closing the protein conformation. Without either residue Tyr137 or Trp204, Fch binding in the protein as mutants Fch-Y137A and Fch-W204A may have a loose conformation, resembling the apo-proteins in proteolysis resistance and migration behaviors in native gel. This study revealed the inconsistence in the key amino acids among Fch-binding proteins from Gram-positive and -negative bacteria, providing interesting findings for understanding the differences between Gram-positive and -negative bacteria in the mechanism of iron uptake via siderophore (Fch) binding and transport.


Subject(s)
Ferrichrome/chemistry , Lipoproteins/chemistry , Periplasmic Proteins/chemistry , Streptococcus pyogenes , Amino Acid Sequence , Amino Acid Substitution , Conserved Sequence , Kinetics , Ligands , Lipoproteins/genetics , Membrane Transport Proteins/chemistry , Membrane Transport Proteins/genetics , Models, Molecular , Molecular Sequence Data , Mutagenesis, Site-Directed , Periplasmic Proteins/genetics , Protein Binding , Protein Stability , Protein Structure, Secondary , Proteolysis , Species Specificity , Structural Homology, Protein , Tryptophan/chemistry , Tryptophan/genetics , Tyrosine/chemistry , Tyrosine/genetics
8.
Luminescence ; 28(2): 244-52, 2013.
Article in English | MEDLINE | ID: mdl-22605685

ABSTRACT

The interaction between cyproheptadine hydrochloride (CYP) and human serum albumin (HSA) was investigated by fluorescence spectroscopy, UV-vis absorption spectroscopy, Fourier transform infrared spectroscopy (FT-IR) and molecular modeling at a physiological pH (7.40). Fluorescence of HSA was quenched remarkably by CYP and the quenching mechanism was considered as static quenching since it formed a complex. The association constants Ka and number of binding sites n were calculated at different temperatures. According to Förster's theory of non-radiation energy transfer, the distance r between donor (human serum albumin) and acceptor (cyproheptadine hydrochloride) was obtained. The effect of common ions on the binding constant was also investigated. The effect of CYP on the conformation of HSA was analyzed using FT-IR, synchronous fluorescence spectroscopy and 3D fluorescence spectra. The thermodynamic parameters ΔH and ΔS were calculated to be -14.37 kJ mol(-1) and 38.03 J mol(-1) K(-1), respectively, which suggested that hydrophobic forces played a major role in stabilizing the HSA-CYP complex. In addition, examination of molecular modeling indicated that CYP could bind to site I of HSA and that hydrophobic interaction was the major acting force, which was in agreement with binding mode studies.


Subject(s)
Cyproheptadine/chemistry , Serum Albumin/chemistry , Spectrum Analysis/methods , Humans , Hydrophobic and Hydrophilic Interactions , Kinetics , Models, Molecular , Protein Binding
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