Difference between revisions of "Part:BBa K1896001"
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* '''A206K''': Monomerizes most GFP variants by disrupting a hydrophobic patch. [3]
 
* '''A206K''': Monomerizes most GFP variants by disrupting a hydrophobic patch. [3]
  
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===References===
 
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# von Stetten, D., Noirclerc-Savoye, M., Goedhart, J., Gadella, T. W., & Royant, A. (2012). Structure of a fluorescent protein from ''Aequorea victoria'' bearing the obligate-monomer mutation A206K. ''Acta Crystallographica Section F: Structural Biology and Crystallization Communications'', 68(8), 878-882.
 
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# Ito, Y., Suzuki, M., & Husimi, Y. (1999). A novel mutant of green fluorescent protein with enhanced sensitivity for microanalysis at 488 nm excitation. ''Biochemical and biophysical research communications'', 264(2), 556-560.
 
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# Crameri, A., Whitehorn, E. A., Tate, E., Stemmer, W. P., Crameri, A., Kitts, P. A., & Kitts, P. A. (1996). Improved green fluorescent protein by molecular evolution using. ''Nat. Biotechnol'', 14(3), 315-319.
 
  
 
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<partinfo>BBa_K1896001 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K1896001 SequenceAndFeatures</partinfo>
  
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===References===
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# von Stetten, D., Noirclerc-Savoye, M., Goedhart, J., Gadella, T. W., &amp; Royant, A. (2012). Structure of a fluorescent protein from ''Aequorea victoria'' bearing the obligate-monomer mutation A206K. ''Acta Crystallographica Section F: Structural Biology and Crystallization Communications'', 68(8), 878-882.
 +
# Ito, Y., Suzuki, M., &amp; Husimi, Y. (1999). A novel mutant of green fluorescent protein with enhanced sensitivity for microanalysis at 488 nm excitation. ''Biochemical and biophysical research communications'', 264(2), 556-560.
 +
# Crameri, A., Whitehorn, E. A., Tate, E., Stemmer, W. P., Crameri, A., Kitts, P. A., &amp; Kitts, P. A. (1996). Improved green fluorescent protein by molecular evolution using. ''Nat. Biotechnol'', 14(3), 315-319.
  
 
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Revision as of 22:56, 12 October 2016


mGFPuv2

Variant of Green Fluorescent Protein (GFP) that contains the following mutations:

  • F99S/M153T/V163A: GFPuv or cycle 3 GFP was optimised for excitation by UV light (360-400nm). [1]
  • S208L: Almost doubles the fluorescent intensity of GFPuv, resulting in GFPuv2. [2]
  • A206K: Monomerizes most GFP variants by disrupting a hydrophobic patch. [3]


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]

References

  1. von Stetten, D., Noirclerc-Savoye, M., Goedhart, J., Gadella, T. W., & Royant, A. (2012). Structure of a fluorescent protein from Aequorea victoria bearing the obligate-monomer mutation A206K. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 68(8), 878-882.
  2. Ito, Y., Suzuki, M., & Husimi, Y. (1999). A novel mutant of green fluorescent protein with enhanced sensitivity for microanalysis at 488 nm excitation. Biochemical and biophysical research communications, 264(2), 556-560.
  3. Crameri, A., Whitehorn, E. A., Tate, E., Stemmer, W. P., Crameri, A., Kitts, P. A., & Kitts, P. A. (1996). Improved green fluorescent protein by molecular evolution using. Nat. Biotechnol, 14(3), 315-319.