Hi Mungo,

The point I was making is that we always follow the work of W. Taylor in this 
since his analysis (published in 1986 in J. Theor. Biol.) is the most complete 
simplified consideration of amino acid properties.  It is derived by projecting 
amino acid subsitution matrices into 2D space and then applying biophysical 
knowledge to the resulting plot (which is dominated by size and hydrophobicity).


https://www.ncbi.nlm.nih.gov/pubmed/3461222.  A few other people have written 
on this subject since then - e.g.:


http://i122server.vu-wien.ac.at/pop/Kosiol_website/pdfs/KosiolGoldmanButtimoreJTB2004.pdf

http://peds.oxfordjournals.org/content/12/9/707.full


but these have not got much traction in the community.


As I said before, Threonine is classed as BOTH Hydrophobic and Polar.  It is 
not the only amino acid like this.


Many text books (and the online resources you point at) take a simplistic view 
that only allows amino acids to have a single property.  For example, they 
typically class Lysine (K) as "Charged".  This hides the fact that Lysine has a 
long aliphatic side chain and is often seen in largely hydrophobic environments 
with the end of the side chain exposed to solvent or in a salt-bridge.  Simple 
text book definitions also usually ignore size which is one of the most 
important biophysical properties of an amino acid.


When I teach about amino acid properties, the first thing I have to explain is 
that the view that amino acid side chains have a single physico-chemical 
property is too simplistic.   I have a powerpoint lecture on this topic if you 
are interested.


In Jalview we could take the view that we should provide people with a range of 
different classifications of the amino acids.  I would prefer that we stick 
with the one that we know from long experience is a reasonable and general 
representation.


I hope this helps?


Geoff.


On 02/11/2016 09:11, Mungo Carstairs (Staff) wrote:

Hi Geoff,


Thanks, I do know what a Venn diagram represents!

Also the page I linked to does show multiple properties for amino  acids.


The question was whether Threonine should be classed as hydrophobic (in which 
case the diagram needs amended) or not (in which case Jalview code needs 
amended).


>From a Google search on amino acid properties, these pages class T as not 
>hydrophobic:

http://www.sigmaaldrich.com/life-science/metabolomics/learning-center/amino-acid-reference-chart.html

http://p53.iarc.fr/AAProperties.aspx

https://www.mcb.ucdavis.edu/courses/bis102/aaprop.html

https://www.thermofisher.com/uk/en/home/life-science/protein-biology/protein-biology-learning-center/protein-biology-resource-library/pierce-protein-methods/amino-acid-physical-properties.html#

http://www.proteinstructures.com/Structure/Structure/amino-acids.html

https://en.wikipedia.org/wiki/Amino_acid#Physicochemical_properties_of_amino_acids

http://www.biology.arizona.edu/biochemistry/problem_sets/aa/Threonine.html


These class T as hydrophobic:

http://www.russelllab.org/aas/

https://www.ncbi.nlm.nih.gov/Class/Structure/aa/aa_explorer.cgi


Question remains, which is it (for Jalview conservation purposes at least)?


thanks


mungo


Mungo Carstairs
Jalview Computational Scientist
The Barton Group
Division of Computational Biology
School of Life Sciences
University of Dundee, Dundee, Scotland, UK.
www.jalview.org<http://www.jalview.org/>
www.compbio.dundee.ac.uk<http://www.compbio.dundee.ac.uk/>
________________________________
From: [email protected]<mailto:[email protected]> 
<[email protected]><mailto:[email protected]> on 
behalf of Geoff Barton <[email protected]><mailto:[email protected]>
Sent: 01 November 2016 17:38:40
To: Jalview Development List
Subject: Re: [Jalview-dev] Is Threonine hydrophobic?


Hi Mungo,


The point of the Venn Diagram is that it shows amino acids to have multiple 
properties.  Threonine sits in the middle of the diagram and has the properties:

Polar, Hydrophobic, Small.


Simple classifications like the one you link to do not capture the fact that 
amino acids exhibit multiple physico-chemical properties.


Rob Russell developed the definitive online resource for amino acid properties: 
 See http://www.russelllab.org/aas/


Geoff.


On 01/11/2016 12:43, Mungo Carstairs (Staff) wrote:

The Venn Diagram (included in Jalview Help as Amino Acid Properties) says that 
it is.


Jalview code, and other reference sources, say it is hydrophilic.

e.g. http://p53.iarc.fr/AAProperties.aspx


Does the diagram need an update?


Thanks,


mungo


Mungo Carstairs
Jalview Computational Scientist
The Barton Group
Division of Computational Biology
School of Life Sciences
University of Dundee, Dundee, Scotland, UK.
www.jalview.org<http://www.jalview.org/>
www.compbio.dundee.ac.uk<http://www.compbio.dundee.ac.uk/>

The University of Dundee is a registered Scottish Charity, No: SC015096


_______________________________________________
Jalview-dev mailing list
[email protected]<mailto:[email protected]>
http://www.compbio.dundee.ac.uk/mailman/listinfo/jalview-dev



--
Geoff Barton | Professor of Bioinformatics | Head of Division of Computational 
Biology
School of Life Sciences | University of Dundee, Scotland, UK | 
[email protected]<mailto:[email protected]>
Tel: +44 1382 385860 | 
www.compbio.dundee.ac.uk<http://www.compbio.dundee.ac.uk> | twitter: @gjbarton


The University of Dundee is registered Scottish charity: No.SC015096


The University of Dundee is a registered Scottish Charity, No: SC015096


--
Geoff Barton | Professor of Bioinformatics | Head of Division of Computational 
Biology
School of Life Sciences | University of Dundee, Scotland, UK | 
[email protected]<mailto:[email protected]>
Tel: +44 1382 385860 | 
www.compbio.dundee.ac.uk<http://www.compbio.dundee.ac.uk> | twitter: @gjbarton


The University of Dundee is registered Scottish charity: No.SC015096


The University of Dundee is a registered Scottish Charity, No: SC015096
_______________________________________________
Jalview-dev mailing list
[email protected]
http://www.compbio.dundee.ac.uk/mailman/listinfo/jalview-dev

Reply via email to