• Bulletin of the Korean Chemical Society
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• v.33 no.2
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• pp.681-684
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• 2012

• Journal of Institute of Control, Robotics and Systems
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• v.14 no.3
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• pp.307-317
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• 2008

Relaxed static stability(RSS) concept has been applied to improve aerodynamic performance of modem version supersonic jet fighter aircraft. Therefore, flight control system are necessary to stabilize an unstable aircraft and provides adequate handling qualities. Also, flight control systems of modem version aircraft employ a safety system to support emergency situations such as a pilot unknown attitude flight conditions of an aircraft in night flight-testing. This situation is dangerous because the aircraft can lose if the pilot not take recognizance of situation. Therefore, automatic recovery system is necessary. The system called the "Pilot Activated Recovery System" or PARS, provided a pilot initiated automatic maneuver capable of an aircraft recoveries in situations of unusual attitudes. This paper addresses the concept of PARS and designed using nonlinear control law design process based on model of supersonic jet trainer. And, this control law is verified by nonlinear analysis and real-time pilot evaluation using in-house software. The result of evaluation reveals that the PARS support recovery of an aircraft unusual attitude and improve a safety of an aircraft.

• Bulletin of the Korean Chemical Society
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• v.14 no.5
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• pp.534-537
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• 1993

• Structural Engineering and Mechanics
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• v.87 no.4
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• pp.363-373
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• 2023

Since the first family of structure-dependent methods can simultaneously integrate unconditional stability and explicit formulation in addition to second order accuracy, it is very computationally efficient for solving inertial problems except for adopting auto time-stepping techniques due to no nonlinear iterations. However, an unusual stability property is first found herein since its unconditional stability interval is drastically different for zero and nonzero damping. In fact, instability might occur for solving a damped stiffness hardening system while an accurate result can be obtained for the corresponding undamped stiffness hardening system. A technique of using a stability factor is applied to overcome this difficulty. It can be applied to magnify an unconditional stability interval. After introducing this stability factor, the formulation of this family of structure-dependent methods is changed accordingly and thus its numerical properties must be re-evaluated. In summary, a large stability factor can result in a large unconditional stability interval but also lead to a large relative period error. As a consequence, a stability factor must be appropriately chosen to have a desired unconditional stability interval in addition to an acceptable period distortion.

• Earthquakes and Structures
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• v.14 no.1
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• pp.45-53
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• 2018

A family of the structure-dependent methods seems very promising for time integration since it can simultaneously have desired numerical properties, such as unconditional stability, second-order accuracy, explicit formulation and numerical dissipation. However, an unusual overshoot, which is essentially different from that found by Goudreau and Taylor in the transient response, has been experienced in the steady-state response of a high frequency mode. The root cause of this unusual overshoot is analytically explored and then a remedy is successfully developed to eliminate it. As a result, an improved formulation of this family method can be achieved.

• Structural Engineering and Mechanics
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• v.60 no.1
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• pp.149-162
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• 2016

Structure-dependent integration methods seem promising for structural dynamics applications since they can integrate unconditional stability and explicit formulation together, which can enable the integration methods to save many computational efforts when compared to an implicit method. A newly developed structure-dependent integration method can inherit such numerical properties. However, an unusual overshooting behavior might be experienced as it is used to compute a forced vibration response. The root cause of this inaccuracy is thoroughly explored herein. In addition, a scheme is proposed to modify this family method to overcome this unusual overshooting behavior. In fact, two improved formulations are proposed by adjusting the difference equations. As a result, it is verified that the two improved formulations of the integration methods can effectively overcome the difficulty arising from the inaccurate integration of the steady-state response of a high frequency mode.

• Proceedings of the Korean Fiber Society Conference
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• 2001.10a
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• pp.361-363
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• 2001

Aromatic pelybenzoxazoles(PBOs) display excellent thermal stability plus good solvent and chemical resistance. Wholly aromatic PBOs, in fact, are soluble only in strong acids(e.g., sulfuric, rmethanesulfonic, triflic, and polyphosphoric acids). However, fully heterocyclized polymers have shown some drawbacks in solubility and processing. This problem of processing is currently being exploited to obtain unusual combinations of physical properties in fibers and films. (omitted)

• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
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• 2001.11b
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• pp.3-6
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• 2001

In common globular proteins, the native form is in its most stable state. However, the native form of inhibitory serpins (serine protease inhibitors) and some viral membrane fusion proteins is in a metastable state. Metastability in these proteins is critical to their biological functions. Our previous studies revealed that unusual interactions, such as side-chain overpacking, buried polar groups, surface hydrophobic pockets, and internal cavities are the structural basis of the native metastability. To understand the mechanism by which these structural defects regulate protein functions, cavity-filling mutations of a 1-antitrypsin, a prototype serpin, were characterized. Increasing conformational stability is correlated with decreasing inhibitory activity. Moreover, the activity loss appears to correlate with the decrease in the rate of the conformational switch during complex formation with a target protease. We also increased the stability of a 1-antitrypsin greatly via combining various stabilizing single amino acid substitutions that were distributed throughout the molecule. The results showed that a substantial increase of stability, over 13 kcal/mol, affected the inhibitory activity with a correlation of 11% activity loss per kcal/mol. The results strongly suggest that the native metastability of proteins is indeed a structural design that regulates protein functions and that the native strain of a 1-antitrypsin distributed throughout the molecule regulates the inhibitory function in a concerted manner.

• Electrical & Electronic Materials
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• v.14 no.12
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• pp.3-6
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• 2001

In common globular proteins, the native form is n its most stable state. However, the native form of inhibitory serpins (serine protease inhibitors) and some viral membrane fusion proteins is in a metastable state. Metastability in these proteins is critical to their biological functions. Our previous studies revealed that unusual interactions, such as side-chain overpacking, buried polar groups, surface hydrophobic pockets, ad internal cavities are the structural basis of the native metastability. To understand the mechanism by which these structural defects regulate protein functions, cavity-filling mutations of $\alpha$1-antitrypsin, a prototype serpin, were characterized. Increasing conformational stability is correlated with decreasing inhibitory activity. Moreover, the activity loss appears to correlate with the decrease in the rate of the conformational switch during complex formation with a target protease. We also increased the stability of $\alpha$1-antitrypsin greatly via combining various stabilizing single amino acid substitutions that were distributed throughout the molecule. The results showed that a substantial increase of stability, over 13 kcal/mol, affected the inhibitory activity with a correlation of 11% activity loss per kcal/mol. The results strongly suggest that the native metastability of proteins is indeed a structural design that regulates protein functions and that the native strain of $\alpha$1-antitrypsin distributed throughout the molecule regulates the inhibitory function in a concerted manner.

• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
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• 2001.11a
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• pp.3-6
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• 2001

In common globular proteins, the native form is in its most stable state. However, the native form of inhibitory serpins (serine protease inhibitors) and some viral membrane fusion proteins is in a metastable state. Metastability in these Proteins is critical to their biological functions. Our previous studies revealed that unusual interactions, such as side-chain overpacking, buried polar groups, surface hydrophobic pockets, and internal cavities are the structural basis of the native metastability. To understand the mechanism by which these structural defects regulate protein functions, cavity-filling mutations of ${\alpha}$1-antitrypsin, a prototype serpin, were characterized. Increasing conformational stability is correlated with decreasing inhibitory activity. Moreover, the activity loss appears to correlate with the decrease in the rate of the conformational switch during complex formation with a target protease. We also increased the stability of ${\alpha}$1-antitrypsin greatly via combining various stabilizing single amino acid substitutions that were distributed throughout the molecule. The results showed that a substantial increase of stability, over 13 kcal/mol, affected the inhibitory activity with a correlation of 11% activity loss per kcal/mol. The results strongly suggest that the native metastability of proteins is indeed a structural design that regulates protein functions and that the native strain of e 1-antitrypsin distributed throughout the molecule regulates the inhibitory function in a concerted manner.