Difference between revisions of "Part:BBa K5301000"
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<partinfo>BBa_K5301000 short</partinfo> | <partinfo>BBa_K5301000 short</partinfo> | ||
| + | ===Usage and Biology=== | ||
Nanodisc technology is a widely applicable approach to render membrane proteins soluble in aqueous solutions in a native-like bilayer environment, where the membrane proteins remain stable and active. The Nanodisc is a non-covalent structure of phospholipid bilayer and membrane scaffold protein (MSP), a genetically engineered protein, which mimics the function of Apolipoprotein A-1 (ApoA-1). The first MSP, MSP1, was engineered with its sequence based on the sequence of A-1, but without the globular N-terminal domain of native A-1. The MSP1E3D1 variant of MSP1 differs from MSP1 in the following facets: (1) It deletes the first 11 amino acids in the Helix 1 portion of the original MSP1 sequence (which is known separately as MSP1D1). The MSP1D1 protein is an N-terminal histidine-tagged protein with a TEV protease cleavage site between the histidine-tag and the protein sequence. (2) It repeats the Helix 4 (H4), Helix 5 (H5) and Helix 6 (H6) sequences of the original MSP1 sequence between the parent Helix 6 (H6) and Helix 7 (H7) segments of MSP1D1. | Nanodisc technology is a widely applicable approach to render membrane proteins soluble in aqueous solutions in a native-like bilayer environment, where the membrane proteins remain stable and active. The Nanodisc is a non-covalent structure of phospholipid bilayer and membrane scaffold protein (MSP), a genetically engineered protein, which mimics the function of Apolipoprotein A-1 (ApoA-1). The first MSP, MSP1, was engineered with its sequence based on the sequence of A-1, but without the globular N-terminal domain of native A-1. The MSP1E3D1 variant of MSP1 differs from MSP1 in the following facets: (1) It deletes the first 11 amino acids in the Helix 1 portion of the original MSP1 sequence (which is known separately as MSP1D1). The MSP1D1 protein is an N-terminal histidine-tagged protein with a TEV protease cleavage site between the histidine-tag and the protein sequence. (2) It repeats the Helix 4 (H4), Helix 5 (H5) and Helix 6 (H6) sequences of the original MSP1 sequence between the parent Helix 6 (H6) and Helix 7 (H7) segments of MSP1D1. | ||
Revision as of 01:29, 30 September 2024
MSP1E3D1 is a genetically engineered protein, which mimics the function of ApoA-I.
Usage and Biology
Nanodisc technology is a widely applicable approach to render membrane proteins soluble in aqueous solutions in a native-like bilayer environment, where the membrane proteins remain stable and active. The Nanodisc is a non-covalent structure of phospholipid bilayer and membrane scaffold protein (MSP), a genetically engineered protein, which mimics the function of Apolipoprotein A-1 (ApoA-1). The first MSP, MSP1, was engineered with its sequence based on the sequence of A-1, but without the globular N-terminal domain of native A-1. The MSP1E3D1 variant of MSP1 differs from MSP1 in the following facets: (1) It deletes the first 11 amino acids in the Helix 1 portion of the original MSP1 sequence (which is known separately as MSP1D1). The MSP1D1 protein is an N-terminal histidine-tagged protein with a TEV protease cleavage site between the histidine-tag and the protein sequence. (2) It repeats the Helix 4 (H4), Helix 5 (H5) and Helix 6 (H6) sequences of the original MSP1 sequence between the parent Helix 6 (H6) and Helix 7 (H7) segments of MSP1D1.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal EcoRI site found at 115
- 12INCOMPATIBLE WITH RFC[12]Illegal EcoRI site found at 115
- 21INCOMPATIBLE WITH RFC[21]Illegal EcoRI site found at 115
Illegal BglII site found at 741
Illegal XhoI site found at 637 - 23INCOMPATIBLE WITH RFC[23]Illegal EcoRI site found at 115
- 25INCOMPATIBLE WITH RFC[25]Illegal EcoRI site found at 115
- 1000COMPATIBLE WITH RFC[1000]