-- %TEACHINGWEB%.GavinSaldanha - 24 Oct 2011
Analyzing the YES-1 gate
This output was generated using the VIENNA pacakge's RNAfold software. This is the structure given if the RNA binds in a Minimum Free Energy (MFE) configuration.
For the OFF position:
input: GGGCGACCCUGAUGAGCUUGAGUUUAGCUCGUCACUGUCCAGGUUCAAUCAGGCGAAACGGUGAAAGCCGUAGGUUGCCC
output: ((((((((((((((((((((....(((.......)))..))))))).))))).....(((((....))))).))))))))
MFE: -37.92 kcal/mol
For the ON position:
input: GGGCGACCCUGAUGAGCUUGAGUUUAGCUCGUCACUGUCCAGGUUCAAUCAGGCGAAACGGUGAAAGCCGUAGGUUGCCC
constraint: .........................xxxxxxxxxxxxxxxxxxxxxx.................................
output: ((((((((.......((((((...........................))))))...(((((....))))).))))))))
MFE: -28.73 kcal/mol
- Structure when On:
- Pairing probability plot when On:
- Structure when Off:
- Pairing probability plot when Off:
Verifying the YES-1 Gate
I really don't know how to do this one. Here is my best guess:
First, the program must read in all necessary inputs. Read in the sequence ($ARGV[0]) and store it, read in the two bounds ($ARGV[1] and $ARGV[2]) and store them.
Go through the sequence between the two bounds and generate DNA-1, the complimentary DNA to that subsequence.
Now run RNAfold on the original sequence. It should match the above diagram of the YES-1 in the off position.
Then run RNAfold on the sequence, giving a constraint that has dots (.) everywhere except between the bounds (which are x's).
This should generate the YES-1 in the on position. If both of these RNAfold outputs match the above graphs, output true for both.
If not output false for whichever plots do not match.
Rfam
- Generated rfam using RNAfold:
- Actual published structure:
These two structures are considerably different. This just shows that although RNAfold can mimic the bonding probabilities to
predict protein structures, such analysis is not always correct. There are some proteins, such as this Rfam, that will not
conform in the way expected based on its sequence. Other factors may contribute to its actual structure, which is probably
much closer to the published one than the predicted structure.

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