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PMID: 8309930 Published · ppublish English Comparative Study Journal Article

Secondary structure prediction of all-helical proteins in two states.

Protein engineering ·Vol. 6 ·No. 8 ·1993-11-00 ·Pages 831-6

Rost B, Sander C

Abstract

Can secondary structure prediction be improved by prediction rules that focus on a particular structural class of proteins? To help answer this question, we have assessed the accuracy of prediction for all-helical proteins, using two conceptually different methods and two levels of description. An overall two-state single-residue accuracy of approximately 80% can be obtained by a neural network, no matter whether it is trained on two states (helix and non-helix) or first trained on three states (helix, strand and loop) and then evaluated on two states. For four test proteins, this is similar to the accuracy obtained with inductive logic programming. We conclude that on the level of secondary structure, there is no practical advantage in training on two states, especially given the added margin of error in identifying the structural class of a protein. In the further development of these methods, it is increasingly important to focus on aspects of secondary structure that aid in the construction of a correct 3-D model, such as the correct placement of segments.

MeSH Terms
Amino Acid Sequence Molecular Sequence Data Neural Networks, Computer Protein Structure, Secondary Software
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Rost B
Protein Design Group, EMBL, Heidelberg, Germany.
Sander C
Article Info
Journal
Protein engineering
Abbr.
Protein Eng
ISSN
0269-2139
Published
1993-11-00
Pages
831-6
Language
English
Region
England
NLM ID
8801484
Subset
IM
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