[gmx-users] How can I reconstruct the system in CGMD simulation?

Justin A. Lemkul jalemkul at vt.edu
Mon Dec 21 20:51:36 CET 2009



rasoul nasiri wrote:
> Hi,
> Thank you for your quick reply.
> 
> Is there another CGFF for this purpose that Gromacs can read it? What is 
> your opinion about CG GO model?
> 

There are several CG models out there, but I don't know much about them.  The 
nice thing about Gromacs is that it can use any force field you can find.

As for Go-models, you've already been given advice on that topic:

http://lists.gromacs.org/pipermail/gmx-users/2009-December/047496.html

-Justin

> Kind regards
> Rasoul
>  
> 
> On Mon, Dec 21, 2009 at 8:23 PM, Justin A. Lemkul <jalemkul at vt.edu 
> <mailto:jalemkul at vt.edu>> wrote:
> 
> 
> 
>     rasoul nasiri wrote:
> 
>         Dear Justin,
>         Thank you for your message.
> 
>         I have found some experimental evidence to suggest that the
>         secondary structure information of protein how change during the
>         reaction of the unfolding. In the other hand, I have percentage
>         of the secondary structure information (%alpha-Helix,
>         %beta-sheet and %Random coil) of the protein at different time
>         of reaction.
>         Could I perform CGMD simulation with MArtini force field for
>         finding the denaturation mechanism of the protein properly?
> 
> 
>     I would be extremely suspicious of any results you get.  As you've
>     been told before, secondary structure is a fixed aspect of a MARTINI
>     CG simulation. Making changes is somewhat arbitrary and may lead to
>     artifacts that you can't anticipate.  Besides, if you only know
>     percentages of secondary structure (from CD I assume?) then you
>     don't really know the structures and sequences that are changing, do
>     you?
> 
>     Net result: this particular CG model is probably not suitable for
>     such a simulation.
> 
>     -Justin
> 
>         Best regards
>         Rasoul
> 
> 
>         On Fri, Dec 18, 2009 at 10:04 PM, Justin A. Lemkul
>         <jalemkul at vt.edu <mailto:jalemkul at vt.edu>
>         <mailto:jalemkul at vt.edu <mailto:jalemkul at vt.edu>>> wrote:
> 
> 
> 
>            rasoul nasiri wrote:
> 
>                Dear Cesar,
>                Thank you for your reply,
> 
>                There are two different kind of water gro in this site
>         (one of
>                them is water.gro in :
>                http://md.chem.rug.nl/~marrink/MARTINI/Coordinates.html
>         <http://md.chem.rug.nl/%7Emarrink/MARTINI/Coordinates.html>
>              
>          <http://md.chem.rug.nl/%7Emarrink/MARTINI/Coordinates.html> and
> 
>                another is water-1bar-303k.gro in :
>                 http://md.chem.rug.nl/~marrink/MARTINI/Tutorial.html
>         <http://md.chem.rug.nl/%7Emarrink/MARTINI/Tutorial.html>
>                <http://md.chem.rug.nl/%7Emarrink/MARTINI/Tutorial.html> . Is
> 
>                there difference between them?
> 
> 
>            Maybe, but if you do sufficient equilibration, it probably
>         won't matter.
> 
> 
>                Can I build water.gro with coarse graining beads (P4) from
>                spc216.gro with using atom2cg.awk script?
> 
> 
>            No.  This has been stated before - the awk script is
>         explicitly for
>            protein. And besides, each "W" CG particle corresponds to
>         about four
>            water molecules, so there is no trivial way to decide how to
>         build
>            the CG water system from spc216.gro.
> 
> 
>                Another question; How can I change secondary structure
>                information during CGMD simulation, If I want to perform CGMD
>                simulation for finding of the folding/unfolding mechanism in
>                proteins completely? Because Martini CGFF consider fix it.
> 
> 
>            You specify the secondary structure when building the initial
>            topology.  As you've been advised already, this "fixed"
>            representation of secondary structure is going to be a major
>            limitation of using the MARTINI force field for your simulations.
>             How do you know that whatever alternate secondary structure
>         you've
>            applied is valid?  If you have some experimental evidence to
>         suggest
>            that certain peptide regions convert between one form and
>         another,
>            that's fine, but how do you know that the pathway taken is not an
>            artifact of your choice to abruptly impose a change in the
>         topology?
> 
> 
>            -Justin
> 
>            --    ========================================
> 
>            Justin A. Lemkul
>            Ph.D. Candidate
>            ICTAS Doctoral Scholar
>            MILES-IGERT Trainee
>            Department of Biochemistry
>            Virginia Tech
>            Blacksburg, VA
>            jalemkul[at]vt.edu <http://vt.edu> <http://vt.edu> | (540)
>         231-9080
> 
>            http://www.bevanlab.biochem.vt.edu/Pages/Personal/justin
> 
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> 
>     -- 
>     ========================================
> 
>     Justin A. Lemkul
>     Ph.D. Candidate
>     ICTAS Doctoral Scholar
>     MILES-IGERT Trainee
>     Department of Biochemistry
>     Virginia Tech
>     Blacksburg, VA
>     jalemkul[at]vt.edu <http://vt.edu> | (540) 231-9080
>     http://www.bevanlab.biochem.vt.edu/Pages/Personal/justin
> 
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-- 
========================================

Justin A. Lemkul
Ph.D. Candidate
ICTAS Doctoral Scholar
MILES-IGERT Trainee
Department of Biochemistry
Virginia Tech
Blacksburg, VA
jalemkul[at]vt.edu | (540) 231-9080
http://www.bevanlab.biochem.vt.edu/Pages/Personal/justin

========================================



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