Talk:Green fluorescent protein: Difference between revisions

Browse history interactively

← Previous edit Next edit →

Content deleted Content added

VisualWikitext

Inline

Revision as of 18:45, 13 November 2008

Template:Wikiproject MCB

GFP is also lurid fun fluorescent aquarium fish

transfectable FP of every color are findable online Blue Green Red are more affordable Yellow is newer

how come this page lacks scientific references? for a subject like GFP, one could find endless supplies of papers...

Since 69.123.68.35 keeps trying to add a Chalfie reference I decided to add a bit of history, including the specific contributions of the 4 main players in the development of GFP. I also fleshed out some detail on the specific mutants that led to EGFP. -AH

GFP Structure

GFP is not a unique structure in fact it has a very typical beta barrel structure seen frequently in membrane proteins such as OmpA. I have corrected that statement. Nick

Nick Hayward (talk) 14:34, 21 January 2008 (UTC)[reply]

Uses

In short, whats it used for? Like many scientific and historical articles on wikipedia, this one goes of at a tangent, without actually describing its importance. You know, scientists don't wear lab coats and drink coffee into the night just to discover a protein they do it for a reward, or its use in the science community. And that reward/use is....? Anyone care to help out?Tourskin 23:47, 17 February 2007 (UTC)[reply]

Agreed, need to flesh out WHY the protein is so important, and the diversity of it's uses. AndrewHires 21:54, 19 February 2007 (UTC)[reply]

Well actually you are wrong. Very often scientists do research on something purely because they are interested in it. Much research is mostly theoretical in the hopes that somehow it will be useful but with no understanding of what that use migh be. In short, often the purpose is merely to expand the body of knowledge we already have and to be able to take what we learn and apply it. I have only heard anecdotally that GFP was discovered because some scienist wanted to figure out why jelly fish glowed. He was given money for this because the scientific community often funds many projects that have biological significance because you never know where the next big discovery will be found and in theory evey piece of information will one day be useful. As for why GFP is important, it can be bound to many biomolecules and now that we know the genes that can encode for it we have investigated how proteins move, interact and degrade, due to the flourscent tag. Also it is used to deterimine when and where certain genes are expressed. On a personal note, I am interested if anyone knows of an industrial, non-biological use. Seems like it should have some applications there. 75.187.39.176 (talk) 16:44, 18 October 2008 (UTC)[reply]

Merge

mGFP should probably be merged as it is only a slight modification of GFP and it may be more informative to have the mGFP content in the main GFP page. It may be a bit confusing though, as m before GFP (or RFP or CFP, etc) more commonly refers to monomeric versions. Any other votes? 66.75.152.122 16:25, 7 May 2007 (UTC)[reply]

Looks like a good merge candidate to me. -- MarcoTolo 20:22, 10 May 2007 (UTC)[reply]

Merged! AndrewHires 01:36, 5 July 2007 (UTC)[reply]

A question

Is the gene itself fluorsecent, or is it only the protein product of the gene that is.

Meaning, if one were to light UV light on a concentration of plasmids containing this gene (but with no nutrient such as arabinose added and no bacteria or other organism), would it be fluorescent? (green?) —Preceding unsigned comment added by 62.107.66.155 (talk • contribs) 15:05, 10 May 2007 (UTC)[reply]

The protein (the green fluorescent protein) is the light-reactive product of the gfp gene. Thus, no, a plasmid containing the gfp gene would not, by itself, fluoresce in the green portion of the visible spectrum. -- MarcoTolo 20:20, 10 May 2007 (UTC)[reply]

Emmision and excitation spectra

A. victorias GFP is excited at 395 nm and 470 nm and emmits light at 509 nm (Maximums). Source: http://public-1.cryst.bbk.ac.uk/PPS2/projects/jonda/chromoph.htm --David Munch 12:30, 10 June 2007 (UTC)[reply]

Primary references are preferred over webpages and the existing references already cover this aspect of GFP. AndrewHires 01:35, 5 July 2007 (UTC)[reply]

Non working link

The link "• Interactive Java applet demonstrating the chemistry behind the formation of the GFP fluorophore." does not work anymore. I wouldn't just remove it, since I dont have time to check up if the link has just changed to something else. --David Munch 20:27, 14 June 2007 (UTC)[reply]

Fixed link - thanks for the heads-up. -- MarcoTolo 20:34, 14 June 2007 (UTC)[reply]

Post translational modification of GFP to make it work

As I understand it, residues of the alpha helix react inside the beta barrel to form the fluorophore, so that the final, fluorescent, protein is chemically modified from the original string of amino acids. Any info about this? 141.5.194.4 12:36, 26 June 2007 (UTC)[reply]

You are correct. The exact side-chain composition induces particular cyclizations to occur. The exact chromophores that are created is gone into in some detail in the Green Fluorescent Protein review by Tsien. Also, papers by Remington on crystallography of various mutants would be a good place to go for greater depth on this issue. AndrewHires 07:17, 4 July 2007 (UTC)[reply]

Errors in history section

GFP and aequorin are totally different proteins (hence the different names). Aequorin is an ion-sensitive indicator, and GFP is (mainly) used to tag individual proteins. There is some GFP history here, and also some good information on the differences between the two proteins and different methods of fluorescent marking in "Molecular Biology of the Cell" (Alberts et al, 4th Ed, 2002). -203.171.67.232 09:38, 10 September 2007 (UTC)[reply]

GFP and Aequorin were not implied to be the same protein, but perhaps the distinction should have been more clear. Modified it. That link is bad, correct link added to External links. I think credit is properly given to all major contributors according to the various reviews, so removed the disputed marking. If someone has additional specific concerns re: history, happy to discuss or add the tag back. AndrewHires 23:54, 17 September 2007 (UTC)[reply]

Species

For all technical purposes the species should be noted as A. aequorea as noted by Osamu Shimomura who is widely credited with discovering GFP. He notes in Green Fluorescent Protein: Properties, Applications, and Protocols, Second Edition Ch 1 that they are in his opinion the same species. Furthermore he says that A. forskalea is also the same species. --Budlight 02:18, 26 October 2007 (UTC)[reply]

Spamming Wikipedia

Biologicalworld.com has spammed wikipedia like no tomorrow. He is a site of only a few pages and a LOT of adsense. Not much information is given except for "protocols" which are not referenced, and cannot be trusted from a site of that quality.

check: Links from Wikipedia

The following have been cleaned up:

en.wikipedia.org/wiki/Plasmid
en.wikipedia.org/wiki/Gel_electrophoresis
en.wikipedia.org/wiki/Green_fluorescent_protein
en.wikipedia.org/wiki/Homology_(biology)
en.wikipedia.org/wiki/HeLa
en.wikipedia.org/wiki/Protease
en.wikipedia.org/wiki/Restriction_enzyme
en.wikipedia.org/wiki/Petri_dish
en.wikipedia.org/wiki/Structural_domain
en.wikipedia.org/wiki/Trypsin
en.wikipedia.org/wiki/Oligonucleotide
en.wikipedia.org/wiki/Transmission_electron_microscope
en.wikipedia.org/wiki/Agar_plate
en.wikipedia.org/wiki/Calcium_phosphate
en.wikipedia.org/wiki/Disulfide_bond
en.wikipedia.org/wiki/Denaturation_(biochemistry)
en.wikipedia.org/wiki/DNA_ligase
en.wikipedia.org/wiki/Wild_type
en.wikipedia.org/wiki/Tissue_culture
en.wikipedia.org/wiki/Transmission_electron_microscopy
en.wikipedia.org/wiki/Reporter_gene
en.wikipedia.org/wiki/Northern_blot

Sciencetalks (talk) —Preceding comment was added at 02:48, 4 January 2008 (UTC)[reply]

Given that it has already been made clear earlier in the article that a number of GFP-expressing organisms have been produced, the entire content of the notes section of this article serves no purpose other than to draw attention to the work of one group of researchers. Perhaps this should also be considered to be spam. —Preceding unsigned comment added by 128.32.173.32 (talk) 23:28, 25 March 2008 (UTC)[reply]

@@ Line 35: / Line 35: @@
 Is the gene itself fluorsecent, or is it only the protein product of the gene that is.
-Meaning, if one were to light UV light on a concentration of plasmids containing this gene (but with no nutrient such as arabinose added and no bacteria or other organism), would it be fluorescent? (green?) {{unsigned|62.107.66.155|15:05, 10 May 2007 (UTC)}}
+Meaning, if one were to light UV light on a concentration of plasmids containing this gene (but with no nutrient such as arabinose added and no bacteria or other organism), would it be fluorescent? (green?) <small><span class="autosigned">—Preceding [[Wikipedia:Signatures|unsigned]] comment added by [[User:62.107.66.155|62.107.66.155]] ([[User talk:62.107.66.155|talk]] • [[Special:Contributions/62.107.66.155|contribs]]) 15:05, 10 May 2007 (UTC)</span></small><!-- Template:Unsigned -->
 :The protein (the green fluorescent protein) is the light-reactive product of the ''gfp'' gene. Thus, no, a plasmid containing the ''gfp'' gene would not, by itself, fluoresce in the green portion of the visible spectrum. -- [[User:MarcoTolo|MarcoTolo]] 20:20, 10 May 2007 (UTC)