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The topology based functional residue classification was obtained by structural alignment of identical proteins using Dali facility [20] and subsequent measure of root mean square deviations (RMSD).
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However, the functional residue-based classification was further extended to the serine protease family, where the classification of query sequences using the method into 3 subfamilies has been described.
7 The respective residues for Ran classification are concentrated close to the C-terminus of the protein.
Per-residue β-sheet classification is used for this comparison since it can be inferred as a common output of all tools; however, AmyloidMutants can provide more rich predictions including super-secondary residue/residue interactions.
In our implementation, the f-score associated to the wild-type and mutant residues in the classification of the subfamilies calculated from the sequences in the PFAM alignments was encoded in the classification vector.
For these five proteins, AmyloidMutants correctly identifies experimentally observed β-sheet regions in 21 of 22 cases (Fig. 4, Table 1)—a per-residue secondary-structure classification sensitivity/specificity of 82%/95% and an average SOV score of 82 (Zelma et al., 1999).
Macnab and Stothers [ 7] developed an algorithm that combined the qualitative NIRS patterns with the maximum flow rate (Qmax) and the postvoid residue (PVR) in the classification of 55 men with LUTS.
Plot shows percentage of classification per residue (i.e. relative number of times a φ,ψ-torsion angle combination is scored as outlier or allowed as defined by phenix.ramalyze).ramalyze
These advances have led to the development of a novel phase diagram based upon net positive and negative charge per residue values for the classification of IDP and IDR sequences [ 129].
However, the number of polar residues according to the classification by Dill and co-workers 11 is somewhat higher in hh Cyt c, and that of hydrophobic residues is correspondingly higher in th Cyt c (Table 1).
However, classification of residues as surface exposed and buried using solely the positions of Cα atoms is highly obscure as the solvent accessibility-based [12] recognition of exposed and buried residues in proteins [2], [13], [14], [15], [16], [17], [18], [19], [20] rely on the availability of side chain positions.
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