The barrel formed by the sheet is slightly oval in cross-section. Along the center of the barrel runs a stretch of amino acids which looks like a very distorted helix . Some of the residues are arranged in a helical pattern . The structure in between is something special : here you find the chromophore which is formed from amino acids Ser65 , Tyr66 and Gly67 by an internal cyclization reaction according to this pathway: The initiation of the cyclization reaction requires the amide N of Gly67 to be in close enough contact to the carbonyl of Ser65, which is the case only after proper folding of the whole protein. The oxidation step generates a large conjugated resonant pi-electron system capable of light absorption. The chromophore is held in place by several amino acids which form a tight hydrogen bond network including some fixed water molecules (distances for possible hydrogen bonds given in Å). Though the wall of the beta-barrel is only one aminoacid thick, it completely shields the chromophore from the surrounding solvent . The barrel got some lids, too, both on bottom and top , to make the whole structure watertight (don't worry about the light - electromagnetic radiation will easily pass the protein layer). Restart this demonstration Literature: F Yang et al, The molecular structure of green fluorescent protein, Nature Biotechnology 14 (1996) 1246-1251 M Ormö et al, Crystal structure of the Aequoria victoria green fluorescent protein, Science 273 (1996) 1392-1395 3-03 - Rolf Bergmann
Though the wall of the beta-barrel is only one aminoacid thick, it completely shields the chromophore from the surrounding solvent . The barrel got some lids, too, both on bottom and top , to make the whole structure watertight (don't worry about the light - electromagnetic radiation will easily pass the protein layer). Restart this demonstration Literature: F Yang et al, The molecular structure of green fluorescent protein, Nature Biotechnology 14 (1996) 1246-1251 M Ormö et al, Crystal structure of the Aequoria victoria green fluorescent protein, Science 273 (1996) 1392-1395 3-03 - Rolf Bergmann