Difference between revisions of "Part:BBa K2302004"
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This sequence encodes a functional protein, liver fatty acid binding protein (L-FABP), which is one of fatty acid binding proteins with a molecular weight of 14-15 kDa.[1] It can reversibly bind long chain fatty acids with hydrogen bond. Its structure consists of two β-sheets, capped by a helix-turn-helix motif. The β-strands are organized into a β-barrel configuration, forming a clam-like structure that encloses a large solvated cavity to form a ligand binding site.[2]FABP1 is primarily expressed in the liver where it is involved in the binding, transport and metabolism of long-chain fatty acids (LCFAs), endocannabinoids, phytocannabinoids, synthetic cannabinoid receptor (CBR) agonists and antagonists, and other hydrophobic molecules.[3] | This sequence encodes a functional protein, liver fatty acid binding protein (L-FABP), which is one of fatty acid binding proteins with a molecular weight of 14-15 kDa.[1] It can reversibly bind long chain fatty acids with hydrogen bond. Its structure consists of two β-sheets, capped by a helix-turn-helix motif. The β-strands are organized into a β-barrel configuration, forming a clam-like structure that encloses a large solvated cavity to form a ligand binding site.[2]FABP1 is primarily expressed in the liver where it is involved in the binding, transport and metabolism of long-chain fatty acids (LCFAs), endocannabinoids, phytocannabinoids, synthetic cannabinoid receptor (CBR) agonists and antagonists, and other hydrophobic molecules.[3] | ||
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===Results=== | ===Results=== | ||
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Figure. 1. The binding capacity of Follower E at different concentrations of fatty acids. | Figure. 1. The binding capacity of Follower E at different concentrations of fatty acids. | ||
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Revision as of 13:40, 27 October 2017
L-FABP,a protein that can bind long chain fatty acids.
This sequence encodes a functional protein, liver fatty acid binding protein (L-FABP), which is one of fatty acid binding proteins with a molecular weight of 14-15 kDa.[1] It can reversibly bind long chain fatty acids with hydrogen bond. Its structure consists of two β-sheets, capped by a helix-turn-helix motif. The β-strands are organized into a β-barrel configuration, forming a clam-like structure that encloses a large solvated cavity to form a ligand binding site.[2]FABP1 is primarily expressed in the liver where it is involved in the binding, transport and metabolism of long-chain fatty acids (LCFAs), endocannabinoids, phytocannabinoids, synthetic cannabinoid receptor (CBR) agonists and antagonists, and other hydrophobic molecules.[3]
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 214
Results
To identify that the functional role of FABP in Follower E, the sample of broken bacteria solution binding with different concentrations of fatty acids was tested using a kit designated for free fatty acids detection. The results showed that Follower E could efficiently bind fatty acids in culture medium when compared to the control, and the binding capacity of Follower E was higher in the medium with 400 μM fatty acids than that of 200 μM fatty acids. The result indicates that the FABP protein produced by Follower E could bind fatty acids as we designed.
Figure. 1. The binding capacity of Follower E at different concentrations of fatty acids.