Difference between revisions of "Part:BBa K2302004"
(→results) |
|||
| (One intermediate revision by the same user not shown) | |||
| Line 4: | Line 4: | ||
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] | ||
| + | |||
| + | <!-- --> | ||
| + | <span class='h3bb'>Sequence and Features</span> | ||
| + | <partinfo>BBa_K2302004 SequenceAndFeatures</partinfo> | ||
| + | |||
===Results=== | ===Results=== | ||
| Line 13: | Line 18: | ||
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. | ||
| − | |||
| − | |||
| − | |||
| + | |||
| + | ===References=== | ||
| + | [1] Frolov. A, Cho. TH and Murphy EJ. Isoforms of rat liver fatty acid binding protein differ in structure and affinity for fatty acids and fatty acyl CoAs. Biochemistry,[J], 1997 May; 36(21) | ||
| + | |||
| + | [2] Tony Velkov,Sara Chuangand Richard Prankerd.An improved method for the purification of rat liver-type fatty acid binding protein from Escherichia coli.Protein Expr Purif,[J],2005Nov;44(1):23–31. | ||
<!-- Uncomment this to enable Functional Parameter display | <!-- Uncomment this to enable Functional Parameter display | ||
Latest revision as of 02:12, 28 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.
References
[1] Frolov. A, Cho. TH and Murphy EJ. Isoforms of rat liver fatty acid binding protein differ in structure and affinity for fatty acids and fatty acyl CoAs. Biochemistry,[J], 1997 May; 36(21)
[2] Tony Velkov,Sara Chuangand Richard Prankerd.An improved method for the purification of rat liver-type fatty acid binding protein from Escherichia coli.Protein Expr Purif,[J],2005Nov;44(1):23–31.