• Journal of the Korean Society for Precision Engineering
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• v.14 no.1
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• pp.205-213
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• 1997

In this study, dynamic analysis of a passenger car is carried out to analyze ride quality over a random road profile. The front suspension of the car is a MacPherson strut type and the rear suspension is a multi- link type. The following five different models are constructed and compared to see the effects of engine vibration and chassis flexibility in the ride quality. (1) one rigid chassis model, (2) a rigid chassis and rigid engine model, (3) a rigid engine and flexible chassis model with one vibration mode, (4) one flexible chassis model with six engine vibration modes and one chassis vibration mode, (5) one flexible chassis model with seven vibration modes and four static correction modes. The result shows that engine vibration modes and the first bending mode of the chassis are important in the ride quality.

• BMB Reports
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• v.38 no.3
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• pp.259-265
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• 2005

Proteins must fold into their correct three-dimensional conformation in order to attain their biological function. Conversely, protein aggregation and misfolding are primary contributors to many devastating human diseases, such as prion-mediated infections, Alzheimer's disease, type II diabetes and cystic fibrosis. While the native conformation of a polypeptide is encoded within its primary amino acid sequence and is sufficient for protein folding in vitro, the situation in vivo is more complex. Inside the cell, proteins are synthesized or folded continuously; a process that is greatly assisted by molecular chaperones. Molecular chaperones re a group of structurally diverse and mechanistically distinct proteins that either promote folding or prevent the aggregation of other proteins. With our increasing understanding of the proteome, it is becoming clear that the number of proteins that can be classified as molecular chaperones is increasing steadily. Many of these proteins have novel but essential cellular functions that differ from that of more 'conventional' chaperones, such as Hsp70 and the GroE system. This review focuses on the emerging role of molecular chaperones in protein quality control, i.e. the mechanism that rids the cell of misfolded or incompletely synthesized polypeptides that otherwise would interfere with normal cellular function.