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Re: Protein Modeling C
Posted: December 5th, 2011, 12:15 pm
by XXGeneration
Shh, don't kill his pride!
![Very Happy :D](./images/smilies/icon_e_biggrin.gif)
Re: Protein Modeling C
Posted: December 5th, 2011, 3:23 pm
by EastStroudsburg13
I'm aware that chain B is easier. >.> My pride is unscathed, though.
My FAQ has been answered! Thank you very much to whoever answered it.
![Very Happy :D](./images/smilies/icon_e_biggrin.gif)
Re: Protein Modeling C
Posted: December 6th, 2011, 2:30 am
by Flavorflav
I am quite surprised by the answer. I would have said go with the PDB, since that is the original data. I suppose this does make it easier for event supervisors, though.
Re: Protein Modeling C
Posted: December 9th, 2011, 2:29 pm
by quizbowl
Hey guys,
Just wondering, what are the exact numbers of residues for chains A and B in Caspace-3.
There are so descrepancies with the numbers listed on the Center for Biomolecular Modeling sheet sent in with the prebuild kit (Chain A=92aa, Chain B=149aa), the PDB bank sequence (Chain A=175aa, 110aa), and jmol counts (Chain A= 148aa, Chain B=91aa).
Can anyone clear this up for us? (Or point out where we're going wrong)
Thanks!
Re: Protein Modeling C
Posted: December 9th, 2011, 2:45 pm
by Luo
quizbowl wrote:Hey guys,
Just wondering, what are the exact numbers of residues for chains A and B in Caspace-3.
There are so descrepancies with the numbers listed on the Center for Biomolecular Modeling sheet sent in with the prebuild kit (Chain A=92aa, Chain B=149aa), the PDB bank sequence (Chain A=175aa, 110aa), and jmol counts (Chain A= 148aa, Chain B=91aa).
Can anyone clear this up for us? (Or point out where we're going wrong)
Thanks!
Unsure how relevant:
http://soinc.org/node/871
Re: Protein Modeling C
Posted: December 9th, 2011, 6:14 pm
by EastStroudsburg13
The numberings for Caspase-3 are 148-296 for Chain A, and 310-401 for Chain B.
In the
Jmol Vizualization, you can select or restrict the specific chains by doing "select *A". There are chains from A through F, so you have to isolate the two you need. Also, if you look on the side, they give you a nice
numbering map.
I'm not sure where you're getting those numbers from. They look vaguely familiar... perhaps they're from last year?
EDIT: I don't think they're last years'. For some reason they look familiar, but I can't determine from where.
Re: Protein Modeling C
Posted: December 10th, 2011, 10:41 am
by njjonas
How do you find active sites in chain A and Chain B???
Re: Protein Modeling C
Posted: December 12th, 2011, 7:11 am
by brobo
Question about something that came up at an invites:
If a protein is made up mostly of Alanine, Valine and Isoleucine, how would the R groups be arranged on the protein and where might this protein be found in a cell:
a. R groups on the inside of the protein's tertiary structure as the protein spans the plasma membrane
b. R groups on the outside of the protein's tertiary structure as the protein spans the plasma membrane
c. R groups on the outside of the protein's tertiary structure while the protein is in the cytoplasm
d. R group positioning is not affected by the local environment
The correct answer is B, but we put A since all those amino acids have hydrophopic sidechains. If they're hydrophobic, then why are the sidechains on the outside of the tetiary structure?
Re: Protein Modeling C
Posted: December 12th, 2011, 7:44 pm
by Phenylethylamine
brobo wrote:Question about something that came up at an invites:
If a protein is made up mostly of Alanine, Valine and Isoleucine, how would the R groups be arranged on the protein and where might this protein be found in a cell:
a. R groups on the inside of the protein's tertiary structure as the protein spans the plasma membrane
b. R groups on the outside of the protein's tertiary structure as the protein spans the plasma membrane
c. R groups on the outside of the protein's tertiary structure while the protein is in the cytoplasm
d. R group positioning is not affected by the local environment
The correct answer is B, but we put A since all those amino acids have hydrophopic sidechains. If they're hydrophobic, then why are the sidechains on the outside of the tetiary structure?
In the part of the protein
spanning the membrane, it is more favorable for hydrophobic groups to be outside, because the phospholipid plasma membrane is, well, lipid – and therefore hydrophobic (nonpolar), so the hydrophobic sidechains want to be in contact with the membrane surroundings.
Re: Protein Modeling C
Posted: December 18th, 2011, 10:33 am
by Allinea
I was at the Boyceville invite, and as we were impounding, I saw one model with a portion of DNA on it. I can't seem to find any sort of DNA in Jmol, unless I can't seem to turn it on right?
So my question is in two parts:
-How do you turn the DNA on in Jmol, if there is any around chains A and B and,
-Anyone have any good ideas for creative additions yet? I'm stumped besides coloring the helices and sheets differently.