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!<br />

hNMc goes through the same procedure, except it ignores the lowest minimum (already<br />

reported by hNMb) and processes all remaining minima as above. If any hinge point is<br />

within five residues of a hinge point corresponding to a lower minimum, the hinge point<br />

corresponding to the higher minimum is discarded.<br />

hNMd (Excluded Region Identifier) works somewhat differently. It is based on the idea<br />

that we may not be able to precisely identify the flexible regions of protein, but we can<br />

perhaps still identify parts of the protein which are rigid, and surmise that the hinge may<br />

lie anywhere except in these rigid regions. For a minimum of<br />

it considers residues<br />

k +1 to<br />

170<br />

!<br />

W located at residues<br />

l " 2 to be part of a structural domain and excludes them<br />

from consideration as a hinge. The process is repeated with the remaining minima<br />

W (k,l). Any ! residues ! that were not excluded after all minima have been considered in<br />

this way are reported as potential hinges.<br />

Lastly, hNMe (Holm and Sander-like hinge predictor) partitions the matrix differently<br />

from NMB with similar goals. The correlation matrix (Equation 2) is partitioned by<br />

separating the residues into two domains much as Holm and Sander did for the contact<br />

!<br />

!<br />

k,l,<br />

k,l of<br />

matrix. A minor adjustment is needed which is explained in the Supplementary Methods<br />

section. This results in a reasonably good predictor which has the added benefit of<br />

assigning each residue to one of two domains, and also has no intrinsic limitation with<br />

respect to number of hinge points. We do not describe this method in great detail,

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