Partial Consensus Design and Enhancement of Protein Function by Secondary-Structure-Guided Consensus Mutations

Biochemistry ◽  
2021 ◽  
Author(s):  
Kohei Kozuka ◽  
Shogo Nakano ◽  
Yasuhisa Asano ◽  
Sohei Ito
2019 ◽  
Vol 15 (4) ◽  
Author(s):  
Tomasz Smolarczyk ◽  
Katarzyna Stapor ◽  
Irena Roterman-Konieczna

AbstractThree-dimensional protein structure prediction is an important task in science at the intersection of biology, chemistry, and informatics, and it is crucial for determining the protein function. In the two-stage protein folding model, based on an early- and late-stage intermediates, we propose to use state-of-the-art secondary structure prediction servers for backbone dihedral angles prediction and devise an early-stage structure. Early-stage structures are used as a starting point for protein folding simulations, and any errors in this stage affect the final predictions. We have shown that modern secondary structure prediction servers could increase the accuracy of early-stage predictions compared to previously reported models.


2013 ◽  
Vol 8 (6) ◽  
pp. e24301 ◽  
Author(s):  
Lee E. Vandivier ◽  
Fan Li ◽  
Qi Zheng ◽  
Matthew R. Willmann ◽  
Ying Chen ◽  
...  

Author(s):  
Qin Wang ◽  
Jun Wei ◽  
Boyuan Wang ◽  
Zhen Li ◽  
Sheng Wang ◽  
...  

Protein secondary structure prediction (PSSP) is essential for protein function analysis. However, for low homologous proteins, the PSSP suffers from insufficient input features. In this paper, we explicitly import external self-supervised knowledge for low homologous PSSP under the guidance of residue-wise (amino acid wise) profile fusion. In practice, we firstly demonstrate the superiority of profile over Position-Specific Scoring Matrix (PSSM) for low homologous PSSP. Based on this observation, we introduce the novel self-supervised BERT features as the pseudo profile, which implicitly involves the residue distribution in all native discovered sequences as the complementary features. Furthermore, a novel residue-wise attention is specially designed to adaptively fuse different features (i.e., original low-quality profile, BERT based pseudo profile), which not only takes full advantage of each feature but also avoids noise disturbance. Besides, the feature consistency loss is proposed to accelerate the model learning from multiple semantic levels. Extensive experiments confirm that our method outperforms state-of-the-arts (i.e., 4.7% for extremely low homologous cases on BC40 dataset).


2011 ◽  
Vol 383-390 ◽  
pp. 4003-4006
Author(s):  
Wen Lung Shu ◽  
Chia Hsuan Lee

Recently, protein-antibody therapeutics becomes a hot search topic. In this paper, all protein interaction data files are collected from INTERPARE. Protein sequence and its secondary structure both are used to build HMM mathematical model. We randomly take 80% data to train positive and negative HMM models and 20% data to test. The accuracy of this approach can reach to 79.80%. This model can further be used to predict protein function sites and predict if a protein interacts with other proteins.


2008 ◽  
Vol 36 (6) ◽  
pp. 1770-1782 ◽  
Author(s):  
Elzbieta Kierzek ◽  
Ryszard Kierzek ◽  
Walter N. Moss ◽  
Shawn M. Christensen ◽  
Thomas H. Eickbush ◽  
...  

2014 ◽  
Vol 1004-1005 ◽  
pp. 853-856
Author(s):  
Hai Xia Long ◽  
Shu Lei Wu ◽  
Yan Lv

Protein structure prediction is a challenging field strongly associated with protein function and evolution determination, which is crucial for biologists. Despite significant process made in recent years, protein structure prediction maintains its status as one of the prime unsolved problems in computational biology. In this study, we have developed a method for protein structure prediction based on 7-state HMM which can reduce the number of states using secondary structure information about proteins for each fold. The QPSO is an efficient optimization algorithm which is used to train profile HMM. Experiment results show that the proposed method is reasonable.


2014 ◽  
Vol 6 (6) ◽  
pp. 1691-1699 ◽  
Author(s):  
Olayinka O. Oshokoya ◽  
Carol A. Roach ◽  
Renee D. JiJi

Determination of protein secondary structure (α-helical, β-sheet, and disordered motifs) has become an area of great importance in biochemistry and biophysics as protein secondary structure is directly related to protein function and protein related diseases.


2020 ◽  
Vol 20 (10) ◽  
pp. 901-909
Author(s):  
Nathanael K. Proctor ◽  
Tugba Ertan-Bolelli ◽  
Kayhan Bolelli ◽  
Ethan W. Taylor ◽  
Norman H.L. Chiu ◽  
...  

Human DNA is a very sensitive macromolecule and slight changes in the structure of DNA can have disastrous effects on the organism. When nucleotides are modified, or changed, the resulting DNA sequence can lose its information, if it is part of a gene, or it can become a problem for replication and repair. Human cells can regulate themselves by using a process known as DNA methylation. This methylation is vitally important in cell differentiation and expression of genes. When the methylation is uncontrolled, however, or does not occur in the right place, serious pathophysiological consequences may result. Excess methylation causes changes in the conformation of the DNA double helix. The secondary structure of DNA is highly dependent upon the sequence. Therefore, if the sequence changes slightly the secondary structure can change as well. These slight changes will then cause the doublestranded DNA to be more open and available in some places where large adductions can come in and react with the DNA base pairs. Computer models have been used to simulate a variety of biological processes including protein function and binding, and there is a growing body of evidence that in silico methods can shed light on DNA methylation. Understanding the anomeric effect that contributes to the structural and conformational flexibility of furanose rings through a combination of quantum mechanical and experimental studies is critical for successful molecular dynamic simulations.


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