๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

New methods for accurate prediction of protein secondary structure

โœ Scribed by John-Marc Chandonia; Martin Karplus


Publisher
John Wiley and Sons
Year
1999
Tongue
English
Weight
122 KB
Volume
35
Category
Article
ISSN
0887-3585

No coin nor oath required. For personal study only.

โœฆ Synopsis


A primary and a secondary neural network are applied to secondary structure and structural class prediction for a database of 681 non-homologous protein chains. A new method of decoding the outputs of the secondary structure prediction network is used to produce an estimate of the probability of finding each type of secondary structure at every position in the sequence. In addition to providing a reliable estimate of the accuracy of the predictions, this method gives a more accurate Q 3 (74.6%) than the cutoff method which is commonly used. Use of these predictions in jury methods improves the Q 3 to 74.8%, the best available at present. On a database of 126 proteins commonly used for comparison of prediction methods, the jury predictions are 76.6% accurate. An estimate of the overall Q 3 for a given sequence is made by averaging the estimated accuracy of the prediction over all residues in the sequence. As an example, the analysis is applied to the target โค-cryptogein, which was a difficult target for ab initio predictions in the CASP2 study; it shows that the prediction made with the present method (62% of residues correct) is close to the expected accuracy (66%) for this protein. The larger database and use of a new network training protocol also improve structural class prediction accuracy to 86%, relative to 80% obtained previously. Secondary structure content is predicted with accuracy comparable to that obtained with spectroscopic methods, such as vibrational or electronic circular dichroism and Fourier transform infrared spectroscopy.


๐Ÿ“œ SIMILAR VOLUMES


Evaluation and improvement of multiple s
โœ James A. Cuff; Geoffrey J. Barton ๐Ÿ“‚ Article ๐Ÿ“… 1999 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 166 KB ๐Ÿ‘ 1 views

A new dataset of 396 protein domains is developed and used to evaluate the performance of the protein secondary structure prediction algorithms DSC, PHD, NNSSP, and PREDATOR. The maximum theoretical Q 3 accuracy for combination of these methods is shown to be 78%. A simple consensus prediction on th

Analyzing protein circular dichroism spe
โœ W. Curtis Johnson ๐Ÿ“‚ Article ๐Ÿ“… 1999 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 44 KB ๐Ÿ‘ 1 views

We have developed an algorithm to analyze the circular dichroism of proteins for secondary structure. Its hallmark is tremendous flexibility in creating the basis set, and it also combines the ideas of many previous workers. We also present a new basis set containing the CD spectra of 22 proteins wi

Improvement of protein secondary structu
โœ Takeshi Kawabata; Junta Doi ๐Ÿ“‚ Article ๐Ÿ“… 1997 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 255 KB ๐Ÿ‘ 1 views

We propose a binary word encoding to improve the protein secondary structure prediction. A binary word encoding encodes a local amino acid sequence to a binary word, which consists of 0 or 1. We use an encoding function to map an amino acid to 0 or 1. Using the binary word encoding, we can statistic