• 한국소음진동공학회논문집
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• 제15권3호
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• pp.354-363
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• 2005

Squeeze film dampers (SFDs) have been commonly used to effectively enhance the dynamic behavior of the rotating shaft supported by rolling element bearings. However, due to the recent trends of high operating speed, high load capacity and light weight in rotating machinery, it is becoming increasingly important to change the dynamic characteristics of rotating machines in operation so that the excessive vibrations, which may occurparticularly when passing through critical speeds or unstable regions, can be avoided. Semi-active type SFDs using magneto-rheological fluid (MR fluid), which responds to an applied magnetic field with a change in rheological behavior, are introduced in order to find its applications to rotating machinery as an effective device attenuating unbalance responses. In this paper, a semi-active SFD using MR fluid is designed, tested, and identified to investigate the capability of changing its dynamic properties such as damping and stiffness.In order to apply the MR-SFD to the vibration attenuation of a rotor, a systematic approach for determining the damper's optimal location is investigated, and also, a control algorithm that could improve the unbalance response characteristics of a flexible rotor is proposed and its control performance is validated with a numerical example.

• Asian Pacific Journal of Cancer Prevention
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• 제14권12호
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• pp.7473-7482
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• 2013

The G-protein coupled receptor 87 (GPR87) is a recently discovered orphan GPCR which means that the search of their endogenous ligands has been a novel challenge. GPR87 has been shown to be overexpressed in squamous cell carcinomas (SCCs) or adenocarcinomas in lungs and bladder. The 3D structure of GPR87 was here modeled using two templates (2VT4 and 2ZIY) by a threading method. Functional assignment of GPR87 by SVM revealed that along with transporter activity, various novel functions were predicted. The 3D structure was further validated by comparison with structural features of the templates through Verify-3D, ProSA and ERRAT for determining correct stereochemical parameters. The resulting model was evaluated by Ramachandran plot and good 3D structure compatibility was evidenced by DOPE score. Molecular dynamics simulation and solvation of protein were studied through explicit spherical boundaries with a harmonic restraint membrane water system. A DRY-motif (Asp-Arg-Tyr sequence) was found at the end of transmembrane helix3, where GPCR binds and thus activation of signals is transduced. In a search for better inhibitors of GPR87, in silico modification of some substrate ligands was carried out to form polar interactions with Arg115 and Lys296. Thus, this study provides early insights into the structure of a major drug target for SCCs.

• Journal of Microbiology and Biotechnology
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• 제34권8호
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• pp.1660-1670
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• 2024

The aim of this study was to modify phytase YiAPPA via protein surficial residue mutation to obtain phytase mutants with improved thermostability and activity, enhancing its application potential in the food industry. First, homology modeling of YiAPPA was performed. By adopting the strategy of protein surficial residue mutation, the lysine (Lys) and glycine (Gly) residues on the protein surface were selected for site-directed mutagenesis to construct single-site mutants. Thermostability screening was performed to obtain mutants (K189R and K216R) with significantly elevated thermostability. The combined mutant K189R/K216R was constructed via beneficial mutation site stacking and characterized. Compared with those of YiAPPA, the half-life of K189R/K216R at 80℃ was extended from 14.81 min to 23.35 min, half-inactivation temperature (T₅₀³⁰) was increased from 55.12℃ to 62.44℃, and T_m value was increased from 48.36℃ to 53.18℃. Meanwhile, the specific activity of K189R/K216R at 37℃ and pH 4.5 increased from 3960.81 to 4469.13 U/mg. Molecular structure modeling analysis and molecular dynamics simulation showed that new hydrogen bonds were introduced into K189R/K216R, improving the stability of certain structural units of the phytase and its thermostability. The enhanced activity was primarily attributed to reduced enzyme-substrate binding energy and shorter nucleophilic attack distance between the catalytic residue His28 and the phytate substrate. Additionally, the K189R/K216R mutant increased the hydrolysis efficiency of phytate in food ingredients by 1.73-2.36 times. This study established an effective method for the molecular modification of phytase thermostability and activity, providing the food industry with an efficient phytase for hydrolyzing phytate in food ingredients.

• 한국소음진동공학회논문집
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• 제23권8호
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• pp.759-769
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• 2013

기동중인 헬리콥터는 공기역학적인 현상에 의하여 발생하는 불규칙 진동과 회전날개의 작동으로 인한 정현파 진동이 합성되어 발생하는 진동, 작업 및 착륙 시 발생하는 충격, 그리고 갑작스런 기동 시 발생하는 가속도와 같은 동적 하중에 노출 된다. 이때 발생하는 진동과 같은 동적 하중은 기체내부로 전달되어 헬리콥터운용에 필요한 전자장비를 가진 한다. 과거에 이러한 현상을 최소화하기 위하여 진동크기 감쇠시키기 위한 완충기를 전자장비의 장착대에 적용하여 왔다. 그러나 헬리콥터의 경우, 저주파에서 정현파 가진이 발생하므로 완충기 적용은 오히려 장착 플레이트 및 전자장비 부품의 파손을 발생시킬 수 있다. 이 연구에서는 완충기를 제거한 장착대를 동적 하중에 강건하며 전자장비에 전달되는 진동크기를 최소화 하도록 설계하였다. 완충기를 제거한 장착 대를 적용 시, 무게와 부피를 획기적으로 줄일 수 있으며 전자장비를 기체에 체결하는 나사 수가 적어짐에 따라 체결작업에 필요한 시간이 감소되는 장점을 갖는다. 최적화 해석에 적용되는 동적 하중을 선정하기 위하여 진동, 충격, 가속도하중을 비교 분석하여 가장 결정적인 동적 하중인 진동에 의한 하중을 선정하였다. 전체모델 유한요소 해석을 통하여 전자장비의 동적 거동을 분석하고 최적화 해석에 필요한 단순화 모델을 구축하였으며, 모달 테스트를 통해서 동특성을 검증하였다. 위상 최적화를 적용하여 강성대비 체적비가 큰 장착대의 형상을 도출한 후 고유진동수, 응력을 제약조건으로 무게가 최소화 되도록 하는 파라미터 최적화를 수행하여 장착대의 최종 형상 및 치수를 결정하였다. 개선모델은 체적 및 질량이 약 13 % 감소하였으며 사용시간은 규격대비 9.2배 증가하였다. 마지막으로 최적화된 장착대를 운용중인 실제 장비에 적용하여 진동환경에 대한 안정성을 평가하였다.