Difference between revisions of "Part:BBa K4759010"

 
 
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<partinfo>BBa_K4759010 short</partinfo>
  
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The 1st – 10th β fold (simply gfp1-10) separates the 11th β fold in the sf gf p structure from the 11th (gfp11), each individually unable to fluoresce, and when gfp1-10 is mixed with a protein containing gfp11 fragment, gfp1-10 actively binds to gfp11 (indicating the higher affinity of gfp1-10 and gfp11) to restore fluorescence activity
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The main principle of bifc, is the fluorescent protein molecules into two separate cannot fluorescent part, respectively fusion with the target protein, when two target protein interact close to each other, the two fluorescent molecule fragments because of physical distance, and complementary, the formation of active fluorescent protein can be detected. Therefore, this fluorescence signal due to complementarity and its strength can be used to indicate whether the two target proteins interact and their strength
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When gfp10 and gfp11 were fused to the target proteins a and b, respectively, and then the two fusion proteins were coexpressed in gfp1-9, due to the affinity between gfp1-9 and gfp11, when gfp10 and gfp11 interact through the target protein, gfp1-9 was also recruited nearby because of the affinity with gfp11, and the three segments were repooled to restore fluorescence activity. This tripartite sf gf p system can be used for protein interaction detection. In addition to the intuitive advantages, the gfp10 and gfp11 are both short peptides, so the influence on the fusion protein structure is probably small. In addition, because it is divided into three parts, the fluorescence background is further reduced, which helps to improve the signal-to-noise ratio of the detection.
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===Usage and Biology===
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<span class='h3bb'>Sequence and Features</span>
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<partinfo>BBa_K4759010 SequenceAndFeatures</partinfo>
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<!-- Uncomment this to enable Functional Parameter display
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===Functional Parameters===
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<partinfo>BBa_K4759010 parameters</partinfo>
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Latest revision as of 17:23, 2 October 2023

GFP10

The 1st – 10th β fold (simply gfp1-10) separates the 11th β fold in the sf gf p structure from the 11th (gfp11), each individually unable to fluoresce, and when gfp1-10 is mixed with a protein containing gfp11 fragment, gfp1-10 actively binds to gfp11 (indicating the higher affinity of gfp1-10 and gfp11) to restore fluorescence activity The main principle of bifc, is the fluorescent protein molecules into two separate cannot fluorescent part, respectively fusion with the target protein, when two target protein interact close to each other, the two fluorescent molecule fragments because of physical distance, and complementary, the formation of active fluorescent protein can be detected. Therefore, this fluorescence signal due to complementarity and its strength can be used to indicate whether the two target proteins interact and their strength When gfp10 and gfp11 were fused to the target proteins a and b, respectively, and then the two fusion proteins were coexpressed in gfp1-9, due to the affinity between gfp1-9 and gfp11, when gfp10 and gfp11 interact through the target protein, gfp1-9 was also recruited nearby because of the affinity with gfp11, and the three segments were repooled to restore fluorescence activity. This tripartite sf gf p system can be used for protein interaction detection. In addition to the intuitive advantages, the gfp10 and gfp11 are both short peptides, so the influence on the fusion protein structure is probably small. In addition, because it is divided into three parts, the fluorescence background is further reduced, which helps to improve the signal-to-noise ratio of the detection.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BglII site found at 48
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]