The most stringent test for predictive methods of protein secondary structure is whether identical short sequences that are known to be present with different conformations in different proteins known at atomic resolution can be correctly discriminated. In this study, we show that the prediction efficiency of this type of segments in unrelated proteins reaches an average accuracy per residue ranging from about 72 to 75% (depending on the alignment method used to generate the input sequence profile) only when methods of the third generation are used. A comparison of different methods based on segment statistics (2nd generation methods) and/or including also evolutionary information (3rd generation methods) indicate that the discrimination of the different conformations of identical segments is dependent on the method used for the prediction. Accuracy is similar when methods similarly performing on the secondary structure prediction are tested. When evolutionary information is taken into account as compared to single sequence input, the number of correctly discriminated pairs is increased twofold. The results also highlight the predictive capability of neural networks for identical segments whose conformation differs in different proteins. (C) 2000 Wiley-Liss, Inc.

Jacoboni I., Martelli P.L., Fariselli P., Compiani M., Casadio R. (2000). Predictions of protein segments with the same aminoacid sequence and different secondary structure: A benchmark for predictive methods. PROTEINS, 41(4), 535-544 [10.1002/1097-0134(20001201)41:4<535::AID-PROT100>3.0.CO;2-C].

Predictions of protein segments with the same aminoacid sequence and different secondary structure: A benchmark for predictive methods

Jacoboni I.;Martelli P. L.;Fariselli P.;Casadio R.
2000

Abstract

The most stringent test for predictive methods of protein secondary structure is whether identical short sequences that are known to be present with different conformations in different proteins known at atomic resolution can be correctly discriminated. In this study, we show that the prediction efficiency of this type of segments in unrelated proteins reaches an average accuracy per residue ranging from about 72 to 75% (depending on the alignment method used to generate the input sequence profile) only when methods of the third generation are used. A comparison of different methods based on segment statistics (2nd generation methods) and/or including also evolutionary information (3rd generation methods) indicate that the discrimination of the different conformations of identical segments is dependent on the method used for the prediction. Accuracy is similar when methods similarly performing on the secondary structure prediction are tested. When evolutionary information is taken into account as compared to single sequence input, the number of correctly discriminated pairs is increased twofold. The results also highlight the predictive capability of neural networks for identical segments whose conformation differs in different proteins. (C) 2000 Wiley-Liss, Inc.
2000
Jacoboni I., Martelli P.L., Fariselli P., Compiani M., Casadio R. (2000). Predictions of protein segments with the same aminoacid sequence and different secondary structure: A benchmark for predictive methods. PROTEINS, 41(4), 535-544 [10.1002/1097-0134(20001201)41:4<535::AID-PROT100>3.0.CO;2-C].
Jacoboni I.; Martelli P.L.; Fariselli P.; Compiani M.; Casadio R.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/906640
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