Amino acid sequence templates derived from recurrent turn motifs in proteins: critical evaluation of their predictive power
- 1 January 1989
- journal article
- research article
- Published by Oxford University Press (OUP) in Protein Engineering, Design and Selection
- Vol. 3 (1) , 23-27
- https://doi.org/10.1093/protein/3.1.23
Abstract
Amino acid sequence patterns suggested to characterize specific recurrent turn conformations in proteins are tested as to their predictive power in a database containing 75 proteins of known structure. Many of these patterns are found to be associated with local structures that differ from the motifs originally used to derive them. It is therefore concluded that, while they could be useful for improving predictions made by other methods, their stand-alone predictive power is poor. The issue of deriving and validating consensus sequence patterns for use in protein structure prediction is raised.This publication has 7 references indexed in Scilit:
- Analysis and prediction of the different types of β-turn in proteinsPublished by Elsevier ,2004
- Structural and sequence patterns in the loops of βαβ unitsProtein Engineering, Design and Selection, 1987
- Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprintJournal of Molecular Biology, 1986
- Interaction of pyrophosphate moieties with .alpha.-helixes in dinucleotide-binding proteinsBiochemistry, 1985
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983
- On the prediction of protein structure: The significance of the root-mean-square deviationJournal of Molecular Biology, 1980
- Structural patterns in globular proteinsNature, 1976