Protein eight-state secondary structure prediction is challenging, but is necessary to determine protein structure and function. Here, we report the development of a novel approach, SPSSM8, to predict eight-state secondary structures of proteins accurately from sequences based on the structural position-specific scoring matrix (SPSSM). The SPSSM has been successfully utilized to predict three-state secondary structures. Now we employ an eight-state SPSSM as a feature that is obtained from sequence structure alignment against a large database of 9 million sequences with putative structural information. The SPSSM8 uses a low sequence identity dataset (9062 entries) as a training set and conditional random field for the classification algorithm. The SPSSM8 achieved an average eight-state secondary structure accuracy (Q8) of 71.7% (Q3, 81.6%) for an independent testing set (463 entries), which had an improved accuracy of 10.1% and 4.6% compared with SSPro8 and CNF, respectively, and significantly improved the accuracy of eight-state secondary structure prediction. For CASP 9 dataset (92 entries) the SPSSM8 achieved a Q8 accuracy of 80.1% (Q3, 83.0%). The SPSSM8 was confirmed as an outstanding predictor for eight-state secondary structures of proteins. SPSSM8 is freely available at http://cal.tongji.edu.cn/SPSSM8.
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http://dx.doi.org/10.1016/j.biochi.2013.09.007 | DOI Listing |
Sci Rep
July 2024
School of Computer Science, Liaocheng University, Liaocheng, 252059, China.
Secondary structure prediction is a key step in understanding protein function and biological properties and is highly important in the fields of new drug development, disease treatment, bioengineering, etc. Accurately predicting the secondary structure of proteins helps to reveal how proteins are folded and how they function in cells. The application of deep learning models in protein structure prediction is particularly important because of their ability to process complex sequence information and extract meaningful patterns and features, thus significantly improving the accuracy and efficiency of prediction.
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August 2022
Arontier Co., Seoul, 06735, Republic of Korea.
Predicting the local structural features of a protein from its amino acid sequence helps its function prediction to be revealed and assists in three-dimensional structural modeling. As the sequence-structure gap increases, prediction methods have been developed to bridge this gap. Additionally, as the size of the structural database and computing power increase, the performance of these methods have also significantly improved.
View Article and Find Full Text PDFACS Omega
June 2022
Institute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.
Parkinson's disease is thought to be caused by aggregation of the intrinsically disordered protein, α-synuclein. Two amyloidogenic variants, A30P, and E46K familial mutants were investigated by wide-line H NMR spectrometry as a completion of our earlier work on wild-type and A53T α-synuclein (Bokor M. et al.
View Article and Find Full Text PDFBiomolecules
November 2021
Institute of Bioinformatics and Systems Biology, National Yang Ming Chiao Tung University, Hsinchu 300, Taiwan.
Secondary structure prediction (SSP) of proteins is an important structural biology technique with many applications. There have been ~300 algorithms published in the past seven decades with fierce competition in accuracy. In the first 60 years, the accuracy of three-state SSP rose from ~56% to 81%; after that, it has long stayed at 81-86%.
View Article and Find Full Text PDFPLoS One
November 2021
Institute of Bioinformatics and Systems Biology, National Chiao Tung University, Hsinchu, Taiwan.
Protein secondary structure prediction (SSP) has a variety of applications; however, there has been relatively limited improvement in accuracy for years. With a vision of moving forward all related fields, we aimed to make a fundamental advance in SSP. There have been many admirable efforts made to improve the machine learning algorithm for SSP.
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