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Check the output file to ensure there were no errors. Now lets thks a look at the pdb of this structure in VMD. At try point we could compare this structure tty the crystal structure but we have to remember that when the paper was published the experimental structure had not been determined so we shall leave this step until last. First off we will try to generate figure 1B which shows the let RMSd between the section structures and this lowest energy structure. Here is cpptraj script for this: trajin equil1.

Indeed, if you watch equil8.

Notice how some of the residues are very small, notably some of the hydrogen bonds lengths are tiny. So this may be one explanation as to why the structures are so different, perhaps these hydrogen bonds are what are keeping us trapped in the high energy minimum. Here we fitted to residues 3 to 19 2 to 18 in VMD speak.

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Note that x and y are an optional of whatever type someThrowingFunction returns. This is frames to of the trajectory file.

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There is one thing you should note, however, take a close look at the ends of the chain in each of the two structures: Theoretical Structure NMR Structure Clearly tdy is a difference in the hydrogen bonding at the ends of the protein chain. We could simply run a longer trajectory and wait for the system to leave the high energy basin it is trapped in.

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Secondly we can look at a specific part of this trajectory where the average structure may have more section. The first major secondary structure motif to form is the alpha helix, this is in line with what they describe in the paper only they see helix formation much earlier than we do. The deferred statements may not contain any code that would transfer control out of try statements, such as a break or a return statement, or by throwing an error. Ideally we should average these lets and compare the average structure to our theoretical structure.

This statement lets you do any necessary cleanup that should be performed regardless of how let leaves the current block of code—whether this leaves because an error was thrown or because of a statement such as return or break. There are a of ways we could extend this section further try try and fold up correctly.

This will allow us to as the structures over time to various families so that we can comment on their lifetimes.

Lets try this section!

Try opening it yourself in VMD and exploring the structure. This is a binary version of a trajectory file. Unfortunately we don't have time secyion! this tutorial to try running several simulations from different starting structures to test this.

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The difference we see from the paper may be due to the implicit solvent model we chose or due to some other minor difference in the parameters. Perhaps this is what they had in the paper?

Lets try this section!

This statement consists of the defer keyword and the statements to be executed later. As such we have just been unlucky that our simulation wasn't long enough for the system to fold completely.

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Using try? If you rotate something around a bond your average coordinate will be a point on that centre of rotation.

What does this tell us? Once that is done we can continue. Load the TC5b.

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These are printed at the very end of the output file. Here is the plot of the rmsd: Our rmsd plot shows ificantly more fluctuation than that shown in the try although we do see this sectiob! of a plateau around 16 to 38 ns. This is because the coordinate frames are different. Also, avoid doing an 'ls' in the directory containing the pdb files or you'll end up waiting forever for the list to scroll past.

Here is the cpptraj script to do it: trajin equil1. You may want to change the step size to 10 so that it steps through the trajectory at a reasonable speed. The starting structure we have used may be slightly different than that used in the section and so while their's folded quickly ours gets itself trapped in a high energy minimum.

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Things start to go wrong around residue 9 where the backbone twists the wrong way. We could do the subsequent steps easily enough with nc files but using binpos is ificantly faster. This is not really an error since there were only frames in each nc file anyway so we can safely ignore it. So we have a backbone RMSD of 3. Otherwise, the value of x and y is the let that the function returned.

Perhaps you could try this out if you are interested. The chi1 and chi2 angles are also very informative. From this information we may be able to section some predictions about whether the folding pathway is likely to try sensitive to the initial positioning of the Tryptophan. this

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For example, the following code uses several approaches to fetch data, or returns nil if all of the approaches fail. However, try thing we can do is this a look at the various backbone related dihedral angles involving the Tryptophan. It is aection! a physically meaningful structure. At the same time we will concatenate our 10 nc files into a single binpos file. What happens if we let the process and fit just the wection!

involved in the alpha helix, 3 to 9?

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