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1.
Cureus ; 14(9): e29674, 2022 Sep.
Article in English | MEDLINE | ID: mdl-36321014

ABSTRACT

We report the perioperative management of a 32-year-old woman with super-morbid obesity (body mass index (BMI) of 60.9 kilograms per meter squared (kg/m2)) who underwent a robotic-assisted total laparoscopic hysterectomy in a hospital that was not specialized for obese patients. She successfully reduced her BMI by 10% using dietary restrictions in five weeks, and her surgery was performed two weeks later by consultation between gynecologists and anesthesiologists. This case demonstrates that the determination of the optimal time for surgery by consultation between physicians is crucial in the care of such a complex patient in hospitals that are not specialized for morbidly obese patients. Weight reduction in the preoperative period should be considered for super-morbid obesity patients with malignant diseases, even if the duration of preoperative optimization is shorter than four to eight weeks.

2.
ACS Omega ; 5(43): 28108-28115, 2020 Nov 03.
Article in English | MEDLINE | ID: mdl-33163793

ABSTRACT

We report a precise measurement of the sensor behavior of the field effect transistor (FET) formed with the MoS2 channel when the channel part is exposed to Cl2 gas. The gas exposure and the electrical measurement of the MoS2 FET were executed with in situ ultrahigh-vacuum (UHV) conditions in which the surface analysis techniques were equipped. This makes it possible to detect how much sensitivity the MoS2 FET can provide and understand the surface properties. With the Cl2 gas exposure to the channel, the plot of the drain current versus the gate voltage (I d-V g curve) shifts monotonically toward the positive direction of V g, suggesting that the adsorbate acts as an electron acceptor. The I d-V g shifts are numerically estimated by measuring the onset of I d (threshold voltage, V th) and the mobility as a function of the dosing amounts of the Cl2 gas. The behaviors of both the V th shift and the mobility with the Cl2 dosing amount can be fitted with the Langmuir adsorption kinetics, which is typically seen in the uptake curve of molecule adsorption onto well-defined surfaces. This can be accounted for by a model where an impinging molecule occupies an empty site with a certain probability, and each adsorbate receives a certain amount of negative charge from the MoS2 surface up to the monolayer coverage. The charge transfer makes the V th shifts. In addition, the mobility is reduced by the enhancement of the Coulomb scattering for the electron flow in the MoS2 channel by the accumulated charge. From the thermal desorption spectroscopy (TDS) measurement and density functional theory (DFT) calculations, we concluded that the adsorbate that is responsible for the change of the FET property is the Cl atom that is dissociated from the Cl2 molecule. The monotonic shift of V th with the coverage suggests that the MoS2 device sensor has a good sensitivity to detect 10-3 monolayers (ML) of adsorption corresponding to the ppb level sensor with an activation time of 1 s.

3.
Proteins ; 86(12): 1231-1241, 2018 12.
Article in English | MEDLINE | ID: mdl-30019770

ABSTRACT

The majority of ß-strands in globular proteins have a right-handed twist and bend. The dominant driving force for ß-strand twisting is thought to be inter-strand hydrogen bonds. We previously demonstrated that for water-soluble proteins, both the twisting and bending of ß-strand are suppressed by the polar side chains of serine, threonine, and asparagine residues. To determine whether this also holds for transmembrane ß-strands, we calculated and statistically analyzed the twist and bend angles of four-residue frames of ß-strands in both transmembrane and water-soluble ß-barrel proteins with known three-dimensional structures. In the case of transmembrane ß-strands, we found that twisting was suppressed even for frames not containing serine, threonine, or asparagine residues. The suppression of twisting in transmembrane ß-strands could be attributed to the propagation of the suppressive effect of serine, threonine, and asparagine residues within a frame to the neighboring, hydrogen-bonded strands under the restriction that all strands in the closed barrel structure must have similar twist angles. A similar tendency was also observed for water-soluble ß-barrel proteins. We previously showed that the dominant driving force for ß-strand bending is hydrophobic interactions involving aromatic residues within and outside the strand. Transmembrane ß-barrels have no hydrophobic core; however, rather hydrophilic residues predominate inside the barrel or the ß-strands of transmembrane ß-barrels have larger bend angles than those of water-soluble ß-barrels. Our results reveal that, in transmembrane ß-barrel proteins, the glycine-aromatic ring motif is important for generating the ß-strand bending necessary for barrel formation.


Subject(s)
Membrane Proteins/chemistry , Models, Molecular , Databases, Protein , Hydrogen Bonding , Hydrophobic and Hydrophilic Interactions , Protein Conformation, beta-Strand , Solubility , Water
4.
Phys Rev Lett ; 109(23): 237209, 2012 Dec 07.
Article in English | MEDLINE | ID: mdl-23368262

ABSTRACT

We have studied the switching behavior of a single Co/Pt multilayer dot under the assistance of rf fields. The switching field monotonically decreases with increasing rf frequency up to a critical frequency. It is found that the reduction of the switching field is more significant than the theoretical prediction based on the single macrospin model. In addition, switching field distribution due to thermal fluctuation is also considerably suppressed. The simulation has revealed that these drastic changes are caused by excitation of large amplitude spin waves in the dot.

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