Turn prediction in proteins using a pattern-matching approach
- 14 January 1986
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 25 (1), 266-275
- https://doi.org/10.1021/bi00349a037
Abstract
We extend the use of amino acid sequence patterns [Cohen, F. E., Abarbanel, R. M., Kuntz, I. D., and Fletterick, R. J. (1983) Biochemistry 22, 4894-4904] to the identification of turns in globular proteins. The approach uses a conservative strategy, combined with a hierarchical search (strongest patterns first) and length-dependent masking, to achieve high accuracy (95%) on a test set of proteins of known structure. Applying the same procedure to homologous families gives a 90% success rate. Straightforward changes are suggested to improve the predictive power. The computer program, written in Lisp, provides a general pattern-recognition language well suited for a number of investigations of protein and nucleic acid sequences.This publication has 33 references indexed in Scilit:
- Prediction of chain turns in globular proteins on a hydrophobic basisNature, 1978
- Preliminary refinement and structural analysis of the Fab fragment from human immunoglobulin new at 2.0 A resolution.Journal of Biological Chemistry, 1978
- The atomic structure of crystalline porcine pancreatic elastase at 2.5 Å resolution: Comparisons with the structure of α-chymotrypsinJournal of Molecular Biology, 1978
- Structure of the semiquinone form of flavodoxin from Clostridium MPJournal of Molecular Biology, 1977
- β-turns in proteinsJournal of Molecular Biology, 1977
- Pseudosymmetry in the structure of myohemerythrin.Journal of Biological Chemistry, 1977
- Structure of myoglobin refined at 2·0 Å resolutionJournal of Molecular Biology, 1977
- Structural patterns in globular proteinsNature, 1976
- A simplified representation of protein conformations for rapid simulation of protein foldingJournal of Molecular Biology, 1976
- THE KINETICS OF FORMATION OF NATIVE RIBONUCLEASE DURING OXIDATION OF THE REDUCED POLYPEPTIDE CHAINProceedings of the National Academy of Sciences, 1961