• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 1998년도 학술발표회
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• pp.16-16
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• 1998

The role of phospholipids in the membrane binding and subsequent insertion of the microsomal protein rabbit cytochrome P450 (P450) lA2 into phospholipid bilayers was investigated. The insertion of P450 lA2 into phospholipid bilayers was determined by the amount of quenching of Trp fluorescence of P450 lA2 by pyrene and brominated and doxyl-labeled phospholipids.(omitted)

• 한국막학회:학술대회논문집
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• 한국막학회 2001년도 추계 총회 및 학술발표회(한국막학회)
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• pp.100-102
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• 2001

• 로봇학회논문지
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• 제16권1호
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• pp.64-71
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• 2021

This paper describes a robotic teleoperation system to perform an accurate needle insertion into a cornea for a separation between the stromal layer and Descemet's membrane during deep anterior lamellar Keratoplasty (DALK). The system can reduce the hand tremor of a surgeon by scaling the input motion, which is the control input of the slave robot. Moreover, we utilize corneal applanation to estimate the insertion depth. The proposed system was validated by performing the layer separation using 25 porcine eyes. The average depth of needle insertion was 742 ± 39.8 ㎛ while the target insertion depth was 750 ㎛. Tremor error was reduced from 402 ± 248 ㎛ in the master device to 28.5 ± 21.0 ㎛ in the slave robot. The rate of complete success, partial success, and failure were 60, 28, and 12%, respectively. The experimental results showed that the proposed system was able to reduce the hand tremor of surgeons and perform precise needle insertion during DALK.

• Molecules and Cells
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• 제27권6호
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• pp.673-680
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• 2009

Conversion of the normal soluble form of prion protein, PrP ($PrP^C$), to proteinase K-resistant form ($PrP^{Sc}$) is a common molecular etiology of prion diseases. Proteinase K-resistance is attributed to a drastic conformational change from ${\alpha}$-helix to ${\beta}$-sheet and subsequent fibril formation. Compelling evidence suggests that membranes play a role in the conformational conversion of PrP. However, biophysical mechanisms underlying the conformational changes of PrP and membrane binding are still elusive. Recently, we demonstrated that the putative transmembrane domain (TMD; residues 111-135) of Syrian hamster PrP penetrates into the membrane upon the reduction of the conserved disulfide bond of PrP. To understand the mechanism underlying the membrane insertion of the TMD, here we explored changes in conformation and membrane binding abilities of PrP using wild type and cysteine-free mutant. We show that the reduction of the disulfide bond of PrP removes motional restriction of the TMD, which might, in turn, expose the TMD into solvent. The released TMD then penetrates into the membrane. We suggest that the disulfide bond regulates the membrane binding mode of PrP by controlling the motional freedom of the TMD.

• 한국미생물학회:학술대회논문집
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• 한국미생물학회 2001년도 추계학술대회
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• pp.97-101
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• 2001

The fusion between viral envelope and target cell membrane is a central step of viral infection, and the fusion proteins located at viral envelope mediate such process. Gp41 of HIV is one of the fusion proteins whose structure and mechanism of membrane fusion had been extensively studied. Functionally important motives of gp41 are the N-terminus fusion peptide, the coiled-coil and the membrane proximal C-peptide regions. The role of these regions during the fusion process had been thoroughly examined. Specially, insertion of the fusion peptide into membrane and conformational change of the coiled-coil and C-peptide regions are assumed to be critical for the fusion mechanism. In addition, the coiled-coil region has been shown to interact with membrane, and the C-peptide region regulates the interaction in a dose dependent manner. Furthermore, fusion defective mutations of the coiled-coil region dramatically changed its binding affinity to membrane. These results suggested that the membrane binding property of the coiled-coil region is important for the fusion activity of gp41, and such property could be modulated by the interaction with the C-peptide region.

• 대한수의학회지
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• 제39권2호
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• pp.327-337
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• 1999

The transposon TnphoA was used to generate avirulent mutants from a type A Pasteurella multocida. A suicide vector plasmid pRT733 carrying TnphoA, having the kanamycin resistant gene and harbored in Escherichia coli K-12 strain SM10(${\lambda}pir$), was mated with streptomycin resistant P. multocida P-1059 strain as recipient. This resulted in the generation of two TnphoA insertion mutants (transconjugants, tc95-a and tc95-b) which were resistant both to kanamycin ($Km^{R}$) and streptomycin ($Sm^{R}$), secreted alkaline phosphatase, and were avirulent to turkeys. Southern blot hybridization using two probes derived from internal fragments of TnphoA, confirmed the insertion of TnphoA into 12.9kb or 13.7kb DNA fragment from the EcoRV digested genomic fragments of transconjugants. The two transconjugants, tc95-a and tc95-b, were distinguishable from their parent strains by differences in ribotypes, and outer membrane protein profiles. TnphoA insertion in both transconjugants also resulted in constitutive expression of a 33Kd iron regulated outer membrane protein (IROMP). The gene encoding $Sm^{R}$ was also located within the same 12.9kb EcoRV genomic fragment from both transconjugants. Furthermore, our finding that the recipient P. multocida P-1059 $Sm^{R}$ strain and both transconjugants were avirulent to turkeys suggest that the either 12.9kb or 13.7kb genomic DNA contains the virulence gene and speculate that the presence of $Sm^{R}$ gene or TnphoA insertion may be responsible for regulating and inactivating the gene(s) encoding virulence in P. multocida.

• Journal of Chest Surgery
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• 제57권3호
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• pp.281-288
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• 2024

Background: Venoarterial extracorporeal membrane oxygenation (ECMO) is a key treatment method used with patients in cardiac arrest who do not respond to medical treatment. A critical step in initiating therapy is the insertion of ECMO cannulas. Peripheral ECMO cannulation methods have been preferred for extracorporeal cardiopulmonary resuscitation (ECPR). Methods: Patients who underwent ECPR at Daegu Catholic University Medical Center between January 2017 and May 2023 were included in this study. We analyzed the impact of 2 different peripheral cannulation strategies (surgical cutdown vs. percutaneous cannulation) on various factors, including survival rate. Results: Among the 99 patients included in this study, 66 underwent surgical cutdown, and 33 underwent percutaneous insertion. The survival to discharge rates were 36.4% for the surgical cutdown group and 30.3% for the percutaneous group (p=0.708). The ECMO insertion times were 21.3 minutes for the surgical cutdown group and 10.3 minutes for the percutaneous group (p<0.001). The factors associated with overall mortality included a shorter low-flow time (hazard ratio [HR], 1.045; 95% confidence interval [CI], 1.019-1.071; p=0.001) and whether return of spontaneous circulation was achieved (HR, 0.317; 95% CI, 0.127-0.787; p=0.013). Low-flow time was defined as the time from the start of cardiopulmonary resuscitation to the completion of ECMO cannula insertion. Conclusion: No statistically significant difference in in-hospital mortality was observed between the surgical and percutaneous groups. However, regardless of the chosen cannulation strategy, reducing ECMO cannulation time was beneficial, as a shorter low-flow time was associated with significant benefits in terms of survival.

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 2003년도 정기총회 및 학술발표회
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• pp.32-32
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• 2003

In the neuron, SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) assembly plays a central role in driving membrane fusion, a required process for neurotransmitter release. In the cytoplasm, vesicular SNARE VAMP2 (vesicle-associated membrane protein 2) engages with two plasma membrane SNAREs syntaxin 1A and SNAP-25 (synaptosome-associated protein of 25 kDa) to form the core complex that bridges two membranes. While various factors regulate SNARE assembly, the membrane also plays the regulatory role by trapping VAMP2 in the membrane. The fluorescence and EPR analyses revealed that the insertion of seven C-terminal core-forming residues into the membrane controls complex formation of the entire core region, even though preceding 54 core-forming residues are fully exposed and freely moving. When two interfacial Trp residues in this region were replaced with hydrophilic serine residues, the mutation supported rapid complex formation.

• Bulletin of the Korean Chemical Society
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• 제28권10호
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• pp.1756-1762
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• 2007

Envelope proteins of virus contain a segment of hydrophobic amino acids, called as fusion peptide, which triggers membrane fusion by insertion into membrane and perturbation of lipid bilayer structure. Potential fusion peptide sequences have been identified in the middle of L or M proteins or at the N-terminus of S protein in the envelope of human hepatitis B virus (HBV). Two 16-mer peptides representing the N-terminal fusion peptide of the S protein and the internal fusion peptide in L protein were synthesized, and their membrane disrupting activities were characterized. The internal fusion peptide in L protein showed higher activity of liposome leakage and hemolysis of human red blood cells than the N-terminal fusion peptide of S protein. Also, the membrane disrupting activity of the extracellular domain of L protein significantly increased when the internal fusion peptide region was exposed to N-terminus by the treatment of V8 protease. These results indicate that the internal fusion peptide region of L protein could activate membrane fusion when it is exposed by proteolysis.

• Transactions on Electrical and Electronic Materials
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• 제14권3호
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• pp.116-120
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• 2013

This paper proposes a novel RF MEMS dc-contact switch with stiff membrane on a quartz substrate. The uniqueness of this work lies in the utilization of a seesaw mechanism to restore the movable part to its rest position. The switching action is done by using separate pull-down and pull-up electrodes, and hence operation of the switch does not rely on the elastic recovery force of the membrane. One of the main problems faced by electrostatically actuated MEMS switches is the high operational voltages, which results from bending of the membrane, due to internal stress gradient. This is resolved by using a stiff and thick membrane. This membrane consists of flexible meanders, for easy movement between the two states. The device operates with an actuation voltage of 6.43 V, an insertion loss of -0.047 dB and isolation of -51.82 dB at 2 GHz.