HIGHLIGHTS
SUMMARY
SNARE proteins consist of motifs of 60-70 amino_acids containing hydrophobic heptad repeats which form coiled-coil structures. The most used approach consists in evaluating whether there are functional motifs and domains in the protein which allow to characterize it starting from its amino_acid sequence and evaluating its belonging to a protein family in which the members have similar three-dimensional structures, similar functions and significant sequence similarities. The extraction of HMM profiles, which allow to identify evolutionary changes in a set of correlated sequences, returns information on the occupancy and position-specific frequency . . .
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