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Literature DB >> 3539099

The predicted secondary structure of enolase.

L Sawyer, L A Fothergill-Gilmore, G A Russell.

Abstract

The results of several secondary-structure prediction programs were combined to produce an estimate of the regions of alpha-helix, beta-sheet and reverse turn for both chicken skeletal-muscle and yeast enolase sequences. The predicted secondary-structure content of the chicken enzyme is 27% alpha-helix and less than 10% beta-sheet, whereas in the yeast enolase a similar helix content but virtually no sheet are predicted. These results are in fair agreement with published experimental estimates of the amount of secondary structure in the yeast enzyme. The enzyme appears to be formed from three domains.

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Year: 1986 PMID： 3539099 PMCID： PMC1146795 DOI： 10.1042/bj2360127

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

16 in total

1. THE REVERSIBLE DENATURATION PROCESSES OF YEAST ENOLASE.

Authors: E W WESTHEAD
Journal: Biochemistry Date: 1964-08 Impact factor: 3.162

2. Prediction of protein conformation.

Authors: P Y Chou; G D Fasman
Journal: Biochemistry Date: 1974-01-15 Impact factor: 3.162

3. Circular dichroism of proteins of known and unknown conformations.

Authors: B Jirgensons
Journal: Biochim Biophys Acta Date: 1970-01-20

4. Algorithms for prediction of alpha-helical and beta-structural regions in globular proteins.

Authors: V I Lim
Journal: J Mol Biol Date: 1974-10-05 Impact factor: 5.469

5. Prediction of the amount of secondary structure in a globular protein from its aminoacid composition.

Authors: W R Krigbaum; S P Knutton
Journal: Proc Natl Acad Sci U S A Date: 1973-10 Impact factor: 11.205

6. Logical analysis of the mechanism of protein folding. I. Predictions of helices, loops and beta-structures from primary structure.

Authors: K Nagano
Journal: J Mol Biol Date: 1973-04-05 Impact factor: 5.469

7. Invariant features of the structure of pancreatic ribonuclease. A test of different predictive models.

Authors: J A Lenstra; J Hofsteenge; J J Beintema
Journal: J Mol Biol Date: 1977-01-15 Impact factor: 5.469

8. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins.

Authors: J Garnier; D J Osguthorpe; B Robson
Journal: J Mol Biol Date: 1978-03-25 Impact factor: 5.469

The predicted secondary structure of enolase.

1. THE REVERSIBLE DENATURATION PROCESSES OF YEAST ENOLASE.

2. Prediction of protein conformation.

3. Circular dichroism of proteins of known and unknown conformations.

4. Algorithms for prediction of alpha-helical and beta-structural regions in globular proteins.

5. Prediction of the amount of secondary structure in a globular protein from its aminoacid composition.

6. Logical analysis of the mechanism of protein folding. I. Predictions of helices, loops and beta-structures from primary structure.

7. Invariant features of the structure of pancreatic ribonuclease. A test of different predictive models.

8. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins.

9. Conformational preferences of amino acids in globular proteins.

10. Snake toxin secondary structure predictions. Structure activity relationships.

1. The complete amino acid sequence of chicken skeletal-muscle enolase.

2. Molecular structure of the human muscle-specific enolase gene (ENO3).