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I thought allosteric meant regulation as a result of induced structural changes.
- That's not the best definition for it, but it does include structural changes. Richard001 07:31, 2 August 2007 (UTC)
When Monod coined the word "allosteric", he used it to describe two binding sites (substrate and effector) having different "structure". By that, he meant they were localized on different parts of the protein (primary structure). It is indeed not meant to describe the fact that the binding site of the effector has a different 3D structure in the T and R states. Nicolas Le Novere (talk) 22:33, 9 November 2008 (UTC)
I didn't nominate the first one, but I suggest we merge both. Richard001 07:33, 2 August 2007 (UTC)
- I agree. Homotropic allosteric modulator should also be merged into this article. Fuzzform 02:29, 22 October 2007 (UTC)
Allosteric enzyme should not be merged with allosteric regulation. Not all the allosteric proteins are enzymes. Counter-examples are channels (e.g. ligand-gate ion channels), transcription factors (e.g. repressor of lactose operon), transporter such as hemoglobin, or signalling regulators such as calmodulin. Nicolas Le Novere (talk) 17:46, 18 April 2008 (UTC)
Article needs simplification
I'm a reasonably intelligent person (earned a college scholarship in engineering), yet couldn't understand this article. You basically have to have studied medicine for this to make sense. For example, look at this sentence at the start of the Pharmacology section :
"Allosteric modulation of a receptor results from the binding of allosteric modulators at a different site (regulatory site) other than of the endogenous ligand (orthosteric ligand) and enhances or inhibits the effects of the endogenous ligand."
I don't recognize the following terms:
- Allosteric modulation
- Regulatory site
- Endogenous ligand
- Orthosteric ligand
Aren't there any ENGLISH words that can be used to describe this process ? If a few unknown words are used I could look them up, but with this many in one sentence (and the strong possibility that looking any of them up in Wikipedia will produce even more confusing terms), I can't see how I can understand such a sentence without first going to medical school. Also, this subject seems just made for illustrations. Aren't there any available ? 22.214.171.124 (talk) 13:49, 30 August 2008 (UTC)
When it comes to the diagrams, I know there are some good ones available in Campbell's Biology textbook. However, I'm not sure if we can use those on Wikipedia. HeartOfCourage (talk) 19:52, 13 April 2014 (UTC)
This article is too complex for the average intro biology student. In order to comprehend this article, you would have to understand the concept of protein dynamics, and the effect of conformational changes. The section that stated, "Allosteric sites allow effectors to bind to the protein, often resulting in conformational change involving protein dynamics.", should be cited. The relationship of between the effector and the active of a given protein should also be elaborated. Morton36 (talk) 22:44, 30 September 2016 (UTC)
I propose that Positive allosteric modulator & Negative allosteric modulator be merged into Allosteric modulation. These two articles say essentially the same thing. I think that the content in both the positive and neagative articles can easily be explained in the context of allosteric modulation, and the Allosteric regulation article is of a reasonable size in which the merging will not cause any problems as far as article size or undue weight is concerned. Andrewaskew (talk) 00:43, 15 June 2012 (UTC)
- This sounds like an excellent idea to me. I'd be even happier if we could pull together an overall article "Allostery", perhaps with several child articles. Dcrjsr (talk) 16:31, 4 July 2012 (UTC)
I do not think they should be merged. I searched specifically to read about positive allosteric modulators and was able to do so much more easily this way. I know positive modulators are less understood than negative ones, but that is no reason to group them together, they are opposite processes acting on neurons. While there is not much information the section at hand, and the individual topics could perhaps both be explained at once, it is much more organized to have them separate for a reader wanting to scan for a particular topic. Plus, keeping them separate will allow for greater adaptability as more information is received and can be posted.
NPOV and clarity
It's good to include the AlloStery Database. But I've edited to fix typos, make it a more appropriate length and less repetitive with the next section, and especially to achieve NPOV. Many of the claims could still use some references (such as for whether allosteric effectors are really more specific and therefore less toxic than other drugs). I also agree with the complaint that this article is not very clearly explained and feel it is definitely confusing between single-chain allostery and multi-subunit allostery. I'll try to come back to it later when I get a chance, since I think it's a very important topic. Dcrjsr (talk) 01:52, 16 August 2012 (UTC)
- Thank you for your efforts. I was just looking at this article because of this blog post. I find the article fairly technical and I have a difficult time understanding this article, most likely because I'm not a protein biochemist. I think it could be simplified or clarified, but I don't understand allostery in the first place! • Jesse V.(talk) 23:49, 19 August 2012 (UTC)
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|I think its good idea to merge both into this article, sice its about allosteric, and the source of allosteric interation is the binding of molecule/molecules to it's allosteric site. And these molecule can actually divded into tow types, one is homoallsteric and another is heteroallosteric. So, it's relevant one.
If I were you I'd check you're definition of the sequential model since its incorrect from another wikipedia page: "This model suggests that the subunits of multimeric proteins have two conformational states. The binding of the ligand causes conformational change. Although the subunits go through conformational changes independently (as opposed to in the MWC model) the switch of one subunit makes the other subunits more likely to change, by reducing the energy needed for subsequent subunits to undergo the same conformational change. In elaboration, the binding of a ligand to one subunit changes the proteins shape, thereby making it more thermodynamically favorable for the other subunits to switch conformation to the high affinity state. It is named KNF after Koshland, Némethy and Filmer." —Preceding unsigned comment added by Cllgnc89 (talk • contribs) 23:02, 11 July 2010 (UTC)
Last edited at 23:03, 11 July 2010 (UTC). Substituted at 07:25, 29 April 2016 (UTC)