| Value |
238
amino acid residues
|
| Organism |
Aequorea victoria |
| Reference |
Nishiuchi Y et al., Chemical synthesis of the precursor molecule of the Aequorea green fluorescent protein, subsequent folding, and development of fluorescence. Proc Natl Acad Sci U S A. 1998 Nov 10 95(23):13549-54. abstract & p.13549 right column 2nd paragraphPubMed ID9811837
|
| Primary Source |
[7] Prasher DC et al., Primary structure of the Aequorea victoria green-fluorescent protein. Gene. 1992 Feb 15 111(2):229-33. [8] Inouye S, Tsuji FI. Aequorea green fluorescent protein. Expression of the gene and fluorescence characteristics of the recombinant protein. FEBS Lett. 1994 Mar 21 341(2-3):277-80. [9] Inouye S, Tsuji FI. Evidence for redox forms of the Aequorea green fluorescent protein. FEBS Lett. 1994 Sep 5 351(2):211-4.PubMed ID1347277, 8137953, 8082767
|
| Method |
Abstract:"The GFP precursor molecule was synthesized from 26 fully protected segments in solution, and the final 238-residue peptide was treated with anhydrous hydrogen fluoride to obtain the precursor molecule of GFP containing two Cys(acetamidomethyl) residues." |
| Comments |
Abstract:"The present paper describes the total chemical synthesis of the precursor molecule of the Aequorea green fluorescent protein (GFP). The molecule is made up of 238 amino acid residues in a single polypeptide chain and is nonfluorescent." p.13549 right column 2nd paragraph:"Aequorea GFP consists of 238 amino acid residues in a single polypeptide chain (primary sources). The native molecule has been shown to regenerate its intrinsic fluorescence from the totally denatured state (ref 10)." |
| Entered by |
Uri M |
| ID |
111747 |