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Comparison List

esGFP

a.k.a. Extra-superfolder GFP

esGFP is a basic (constitutively fluorescent) fluorescent protein published in 2016, derived from Aequorea victoria.

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Oligomerization Organism Molecular Weight Cofactor
? Aequorea victoria 26.8 kDa -

FPbase ID: FZZ8D

Attributes

This protein does not yet have any fluorescent states assigned. Submit a change.

Photostability

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esGFP Sequence

BLAST

esGFP was derived from Superfolder GFP with the following mutations: L42I/F46L/L64C/T65G/S72A/Y106F/L119T/E124K/N149K/L194R/L207I/S208L/K209E/L221H

MSKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKITLKLICTTGKLPVPWPTLVTTCGYGVQCFARYPDHMKRHDFFKSAMPEGYVQERTISFKDDGTFKTRAEVKFEGDTIVNRIKLKGIDFKEDGNILGHKLEYNFNSHKVYITADKQKNGIKANFKIRHNVEDGSVQLADHYQQNTPIGDGPVRLPDNHYLSTQSVILEDPNEKRDHMVLHEFVTAAGITHGMDELYK

Structure

Deposited: ,
Chromophore:

Excerpts

No excerpts have been added for esGFP
Excerpts are snippets from publications that capture key information about this protein that does not easily fit into one of the existing fields (such as a summary, motivation, or observation).

Primary Reference

The mechanism of folding robustness revealed by the crystal structure of extra-superfolder GFP

Choi Jy, Jang T-H, Park Hh

(2016). FEBS Letters, 591(2) , 442-447. doi: 10.1002/1873-3468.12534. Article   Pubmed

Additional References

  1. Engineering Protein Sequence Composition for Folding Robustness Renders Efficient Noncanonical Amino acid Incorporations

    Nagasundarapandian S, Merkel L, Budisa N, Govindan R, Ayyadurai N, Sriram S, Yun H, Lee S-G

    (2010). ChemBioChem, 11(18) , 2521-2524. doi: 10.1002/cbic.201000380. Article   Pubmed

External Resources

Change history

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