What is gfp protein

PDB builds introductory materials to help beginners get started in the subject "", as in an entry level course as well as resources for extended learning. Toggle navigation PDB Educational portal of. Molecule of the Month. The green fluorescent protein, shown here from PDB entry 1gfl , is found in a jellyfish that lives in the cold waters of the north Pacific. The jellyfish contains a bioluminescent protein-- aequorin--that emits blue light.

The green fluorescent protein converts this light to green light, which is what we actually see when the jellyfish lights up. Solutions of purified GFP look yellow under typical room lights, but when taken outdoors in sunlight, they glow with a bright green color.

The protein absorbs ultraviolet light from the sunlight, and then emits it as lower-energy green light.

You might be saying: who cares about this obscure little green protein from a jellyfish? It turns out that GFP is amazingly useful in scientific research, because it allows us to look directly into the inner workings of cells. It is easy to find out where GFP is at any given time: you just have to shine ultraviolet light, and any GFP will glow bright green. So here is the trick: you attach the GFP to any object that you are interested in watching.

For instance, you can attach it to a virus. Then, as the virus spreads through the host, you can watch the spread by following the green glow.

Or, you can attach it to a protein, and watch through the microscope as it moves around inside cells. GFP is a ready-made fluorescent protein, so it is particularly easy to use. Most proteins that deal with light use exotic molecules to capture and release photons. For instance, the opsins in our eyes use retinol to sense light see the Molecule of the Month on bacteriorhodopsin. These "chromophores" must be built specifically for the task, and carefully incorporated into the proteins.

GFP, on the other hand, has all of its own light handling machinery built in, constructed using only amino acids. It has a special sequence of three amino acids: serine-tyrosine-glycine sometimes, the serine is replaced by the similar threonine. When the protein chain folds, this short segment is buried deep inside the protein. Transgenic mice can be labeled with GFP, which is then easily observed in their offspring just by exposing them to blue or UV light, as seen in Fig.

GFP can be fused to other proteins, effectively making those proteins fluorescent. This allows any protein to be localized and tracked using standard fluorescent microscopy, by shining a blue light on the cells, the protein of interest will fluoresce back with a green light. GFP in live-cell experiments : the classic green fluorescent molecule is fluorescein isothiocyanate FITC , but this is toxic to cells and cannot be used directly without first fixing the cells or causing unavoidable damage.

GFP is far less harmful as it is a naturally-occurring protein and can be used in experiments on live cells while causing virtually no damage, especially if it is passed on to offspring. GFP in advanced microscopy applications. GFP is modifiable , as the genetic and amino acid code for GFP is well understood it has been subject to several modifications. Firstly GFP was modified to produce enhanced GFP eGFP , which has increased fluorescence intensity, greater photostability, more convenient excitation peaks and higher efficiency at room temperature.

Some standout modifications include mCherry red , Citrine and Venus yellow , and Cerulean cyan to name a few. Entire families of fluorescent proteins now exist, all derived from the original GFP, as seen in Fig. Constant improvements on GFP over time have caused fluorescence microscopy and research to move forward, due to the highly flexible nature of GFP and the large body of research based on using GFP and its many variants.

What is GFP? Mulashkin, Egor S. Bulavko, Tatiana M. Zakharova, Alexander V. Journal of Chemical Information and Modeling , 60 12 , Knutson, Aimee A. Sanford, Colin S. Swenson, Megan M. Korn, Brea A.

Manuel, Jennifer M. Journal of the American Chemical Society , 41 , Chemical Reviews , 7 , The Journal of Physical Chemistry B , 13 , Bioconjugate Chemistry , 31 1 , Journal of the American Chemical Society , 2 , Grigorenko, Igor V.

Polyakov, Anna I. Krylov, Alexander V. The Journal of Physical Chemistry B , 42 , Nemukhin, Bella L. Grigorenko, Maria G. Khrenova, Anna I. The Journal of Physical Chemistry B , 29 , Journal of the American Chemical Society , 24 , The Journal of Physical Chemistry A , 22 , Baranov, Longteng Tang, Nadezhda S.

Baleeva, Alexander Yu. Smirnov, Ilia V. Yampolsky, Kyril M. Solntsev, Chong Fang. The Journal of Physical Chemistry B , 17 , Kraus, Jacob W. The Journal of Physical Chemistry B , 11 , The Journal of Physical Chemistry B , 10 , Journal of the American Chemical Society , 9 , The Journal of Physical Chemistry B , 50 , The Journal of Physical Chemistry B , 49 , The Journal of Physical Chemistry A , 28 , Wolstenholme, Gregory C.

Hoelzel, Hemant P. Bioconjugate Chemistry , 29 4 , Journal of Chemical Theory and Computation , 14 4 , Organic Letters , 20 7 , Grigorenko , Anna I. Krylov , and Alexander V. Journal of the American Chemical Society , 30 , The Journal of Physical Chemistry B , 18 , Campbell , and Chong Fang. The Journal of Physical Chemistry B , 14 , The Journal of Physical Chemistry C , 8 , Hailes , Philip C.

Bulman Page , Stephen R. The Journal of Physical Chemistry Letters , 8 4 , Bogdanov , Bella L. Grigorenko , Ksenia B. Bravaya , Alexander V. Nemukhin , Konstantin A. Lukyanov , and Anna I. Chemical Reviews , 2 , Journal of Chemical Theory and Computation , 12 11 , Hratchian , Michael J. Frisch , and Nadia Rega. Journal of Chemical Theory and Computation , 12 10 , The Journal of Physical Chemistry B , 37 , Journal of the American Chemical Society , 31 , The Journal of Physical Chemistry B , 19 , Ryan , Pablo G.

Jambrina , Edina Rosta , and Oren A. Journal of the American Chemical Society , 18 ,