Circularly permuted variants of the green fluorescent protein
Open Access
- 27 August 1999
- journal article
- Published by Wiley in FEBS Letters
- Vol. 457 (2) , 283-289
- https://doi.org/10.1016/s0014-5793(99)01044-3
Abstract
Folding of the green fluorescent protein (GFP) from Aequorea victoria is characterized by autocatalytic formation of its p‐hydroxybenzylideneimidazolidone chromophore, which is located in the center ...Keywords
This publication has 35 references indexed in Scilit:
- Random circular permutation of DsbA reveals segments that are essential for protein folding and stabilityJournal of Molecular Biology, 1999
- Chromophore Formation in Green Fluorescent ProteinBiochemistry, 1997
- MOLMOL: A program for display and analysis of macromolecular structuresJournal of Molecular Graphics, 1996
- Deletion mapping of the Aequorea victoria green fluorescent proteinGene, 1996
- Primary structure of the Aequorea victoria green-fluorescent proteinGene, 1992
- Correct Folding of Circularly Permuted Variants of a βα Barrel Enzyme in VivoScience, 1989
- Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectorsGene, 1985
- Amino and carboxy-terminal regions in globular proteinsJournal of Molecular Biology, 1983
- Circular and circularly permuted forms of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1983
- Renaturation of Aequorea green-fluorescent proteinBiochemical and Biophysical Research Communications, 1981