Structure and Function of Green Fluorescent Protein

About this project

These webpages about Green Fluorescent Protein (GFP) have been developped as a dissertation project for the Principles of Protein Structure Using the Internet course, in which I have participated as a student. You may also want to have a look at my colleagues' projects.

At this point I would like to thank all the tutors, consultants and fellow students, who made this course work - and it has often been great fun, too! I am also indebted to Prof. George Phillips, who has kindly given me the coordinate file of GFP prior to its PDB release. Finally, I am grateful to Horst-Joachim Schirra for his help with corel-draw and for patiently discussing many ideas of this project despite his own heavy workload.

The project is best viewed with Netscape2, but apart from a few messy sub- and superscripts Netscape1 should be okay as well.
Feel free to mail me your comments!


GFP is an extraordinary protein in many respects: It is fluorescent and its fluorophore is made up of modified amino acid residues. Moreover it is the first known example of a Förster cycle within the core of a protein. Furthermore its crystal structure has recently been solved and the protein turned out to have a new structural motif, called the beta-can. On the following pages I will set out to discuss some of the most interesting features of this unique protein, starting out with its function in the introduction, followed by a view on the more or less isolated chromophore and finally presenting the three-dimensional structure of this fascinating protein.


Introduction The Chromophore of GFP The 3D Structure of GFP References

Next [Introduction]

Silke Jonda's PPS2 project
Structure and Function of GFP
updated 28.11.96