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Protein Modeling C
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- EastStroudsburg13
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Re: Protein Modeling C
I'm aware that chain B is easier. >.> My pride is unscathed, though.
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My FAQ has been answered! Thank you very much to whoever answered it.
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Re: Protein Modeling C
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.
- quizbowl
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Re: Protein Modeling C
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!
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!
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Re: Protein Modeling C
Unsure how relevant: http://soinc.org/node/871quizbowl 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!
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- EastStroudsburg13
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Re: Protein Modeling C
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?![Confused :?](./images/smilies/icon_e_confused.gif)
EDIT: I don't think they're last years'. For some reason they look familiar, but I can't determine from where.
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?
![Confused :?](./images/smilies/icon_e_confused.gif)
EDIT: I don't think they're last years'. For some reason they look familiar, but I can't determine from where.
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- brobo
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Re: Protein Modeling C
Question about something that came up at an invites:
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?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
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Re: Protein Modeling C
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.brobo wrote:Question about something that came up at an invites: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?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
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- Allinea
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Re: Protein Modeling C
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.
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.
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