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| Title: | Protein secondary structure prediction continues to rise |
| Author: | Burkhard Rost |
| Quote: | J Structural Biology, 2001, 134:204-218 |
Methods predicting protein secondary structure have improved substantially
in the 90's through using evolutionary information taken from
the divergence of proteins in the same structural family. Recently,
the evolutionary information resulting from improved searches
and larger databases has again boosted prediction accuracy by
more than four percentage points to its current height around
76% of all residues predicted correctly in one of the three states
helix, strand, other. The last year also brought successful new
concepts to the field. These new methods may be particularly interesting
in light of the improvements achieved through simply combining
existing methods. Divergent evolutionary profiles not only contain
enough information to substantially improve prediction accuracy,
but even to correctly predict long stretches of identical residues
observed in alternative secondary structure states depending on
non local conditions. An example is a method automatically identifying
structural switches, and thus finding a remarkable connection
between predicted secondary structure and aspects of function.
Secondary structure predictions are increasingly becoming the
working horse for numerous methods aiming at predicting protein
structure and function. Is the recent increase in accuracy significant
enough to make predictions even more useful? Since the recent
improvement yields a better prediction of segments, and in particular
of beta-strands, I believe the answer is affirmative. What is
the limit of prediction accuracy? We shall see.
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