MOLECULAR DYNAMIC SIMULATION OF B DOMAIN OF HUMAN PROTEIN DISULFIDE ISOMERASE IN 8 M UREA
Protein folding mechanism is an important aspect in chemistry, especially in biochemistry. The protein folding mechanism provide informations about how the native structure of the protein was formed and also how the most stable structure of the protein. In this research we have performed unfolding s...
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| Format: | Final Project |
| Language: | Indonesia |
| Online Access: | https://digilib.itb.ac.id/gdl/view/11304 |
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| Institution: | Institut Teknologi Bandung |
| Language: | Indonesia |
| Summary: | Protein folding mechanism is an important aspect in chemistry, especially in biochemistry. The protein folding mechanism provide informations about how the native structure of the protein was formed and also how the most stable structure of the protein. In this research we have performed unfolding simulation of B domain of Protein Disulfide Isomerase (PDI) in 8 M Urea solution at 500 K. The objective of this study is to elucidate the unfolding mechanism of the enzyme. The result of this simulation revealed that the unfolding mechanism of B domain PDI was a two state transition processes. This observation is similiar to the experimental result which have been reported previously that proved the simulation results are valid. Further inspection to the simulation trajectory suggested that folding mechanism of B domain of human PDI followed the model of Nucleation Condensation. This simulation thus provide insight to the molecular process of PDI folding. <br />
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