Talk:Intrinsically disordered proteins

message: I was confused by the following in the section "Identification of intrinsically unstructured proteins"
:Intrinsically unfolded proteins, once purified, can be identified by various experimental methods. Folded proteins have a high density (partial specific volume of 0.72-0.74 mL/g) and commensurately large radius of gyration.
I thought that, if unfolded proteins have relatively higher density, then would they have smaller radius of gyration instead of larger. Could anybody help explain this to me? Thanks!
--Dai mingjie (talk) 16:00, 6 September 2010 (UTC)
replies: text: You are right, I think it's an error in the text. I will correct it. --Cyclopiatalk 18:09, 6 September 2010 (UTC)
thread_title:  Question about experimental identification 

message: I am having a problem with the following statement "Sequence signatures of disorder: Intrinsically unstructured proteins are characterized by a low content of bulky hydrophobic amino acids and a high proportion of polar and charged amino acids."
This statement is not true for many disordered protein fibers like collagen, elastin, dragline spider silk and mussel byssus.  In particular Elastin's material property's likely come from the high number of bulky hydrophobic amino acids in its sequence.  For a good elastin ref look up any paper by Dan Urry.
Also this wiki post needs a discussion about how the definition of "structured" vs. "disordered" is a matter of time scale.  It is true that disordered proteins have sub-microsecond conformational dynamics but the underlining chemical reactions that these proteins motivate occur on picosecond times scales.  So it is more appropriate to say that these proteins might be transiently structured as opposed to saying that these proteins are completely unstructured.  More recent ultrafast spectroscopic  data has shown that for many of these highly mobile systems there still remains innate structural preferences that persist for longer then the picosecond time scale required for a typical chemical reaction.
::It's more about lack of packed globular/crystal structure rather than saying the molecule has no intrinsic structure. A given disordered region is an ensemble of many short lived more stable 3D structures that don't form a self contained stable hydrophobic core even on short time scales. A key point is that if you wanted to use X-ray crystallography to see these structures you would be there for quite some time trying, and this is not a failing of the methods employed. Also the literature does describe the full spectrum of unfolded/disordered -upto-> structured, with the concept of molten globules where secondary structure is kept in a loose ensemble that is quite flexible and often part of a more stable domain. -- MattOates (Ulti) 17:43, 21 September 2012 (UTC)
thread_title: Sequence signatures of disorder

message: I propose that we move this article to Intrinsically Disordered Proteins.
*IDP is the more commonly used term
*IUPs are an extreme case of IDPs and so could nest within that article
*A large mount of the current article deals with IDPs anyway.
See the discussion on the creation of a separate article for intrinsically disordered proteins here. Does anyone have any objections to the idea? T. Shafee (Evo&Evo) (talk) 09:35, 14 March 2014 (UTC)
thread_title:  Article move to [[Intrinsically Disordered Proteins]] 

message: Not to waste people effort Lukaskoz (talk) 07:55, 23 October 2014 (UTC)
replies: text: great initiative in principle. Only I doubt, many people will read the talk part of this Wiki. Dont you think it will be easier to create a new IDP page (sort of pretenting there is no IUP wiki) and then let the WIKI-community decide whats best (merge/coexistence or whatever)? David P Minde (talk) 17:16, 18 March 2014 (UTC)
replies: text: I more meant that the list shouldn't appear on the main page as it is, but rather that the references would appear in the rest of the article. E.g. references to Keith Dunker will appear in the history section, references to Ursula Jakob's work would appear in the coupled folding and binding section. All the information from the list would appear when the lab's work is summarised in the article and the list itself coud be removed. T. Shafee (Evo&Evo) (talk) 23:24, 19 October 2014 (UTC)

text: Hi, I am wondering whether it makes sense to include such a list in this article.  Deciding which labs are pioneering is very subjective. I don't recall seeing such a list elsewhere on Wikipedia. I realise a lot of work has gone into this, but perhaps the word pioneering should be replaced with something else. But if it was simply list of labs involved in IDP research, then I think we may get hundreds of entries.  So perhaps its best to create a new article called IDP Research Labs and move this content there. Alexbateman (talk) 11:56, 15 April 2014 (UTC)
thread_title:  IDP labs and references 

message: The lead and only figure in this article is terribly pixelated. Does anyone have a better image to include? There must be some out there.T. Shafee (Evo&Evo) (talk) 23:23, 19 October 2014 (UTC)
thread_title:  New/improved image? 

message: Substituted at 18:23, 17 July 2016 (UTC)
thread_title: Assessment comment