• Journal of the Korean Magnetic Resonance Society
• /
• v.15 no.1
• /
• pp.69-79
• /
• 2011

HP0827 has two RNP motif which is a very common protein domain involved in recognition of a wide range of ssRNA/DNA.We acquired 3D NMR spectra of HP0827 which shows well dispersed and homogeneous signals which allows us to assign 98% of all $^1H_N$, $^{15}N$, $^{13}C_{\alpha}$, $^{13}C_{\beta}$ and $^{13}C$=O resonances and 90% of all sidechain resonances. The sequence-specific backbone resonance assignment of HP0827 can be used to gain deeper insights into the nucleic acids binding specificity of HP0827 in the future study. Here, we report secondary structure prediction of HP0827 derived from NMR data. Additionally, ssRNA/DNA binding assay studies was also conducted. This study might provide a clue for exact function of HP0827 based on structure and sequence.

• Asian-Australasian Journal of Animal Sciences
• /
• v.19 no.6
• /
• pp.763-768
• /
• 2006

Genetic and pharmacological studies in mice have demonstrated a complementary role for the melanocortin 4 receptor (MC4R) in the control of food intake, energy balance and body weight. This study was designed to investigate the associations of a MC4R gene polymorphism on chicken growth and body composition traits in broiler lines divergently selected for abdominal fat. A SNP (G54C) was found in CDS region of chicken MC4R gene. The analysis of the least squares and variance revealed a significant association between the G54C SNP and BW, CW and SL at 7 wk of age, and there were significant differences in different genotypes (p<0.05). The results from protein secondary structure prediction and tertiary structure prediction showed that it appeared a helix in $13^{th}$ amino acid and two strands at $14^{th}$ and $15^{th}$ amino acid in mutant protein, respectively. It maybe induce the change of the activity or function of MC4R gene in poultry.

• Proceedings of the Korean Information Science Society Conference
• /
• 2007.10b
• /
• pp.22-27
• /
• 2007

Phosphorylation is one of the most important post translational modifications which regulate the activity of proteins. The problem of predicting phosphorylation sites is the first step of understanding various biological processes that initiate the actual function of proteins in each signaling pathway. Although many prediction methods using single or multiple features extracted from protein sequences have been proposed, systematic data integration approach has not been applied in order to improve the accuracy of predicting general phosphorylation sites. In this paper, we propose an optimal way of integrating multiple features in the framework of multiple kernel learning. We optimally combine seven kernels extracted from sequence, physico-chemical properties, pairwise alignment, and structural information. Using the data set of Phospho. ELM, the accuracy evaluated by 5-fold cross-validation reaches 85% for serine, 85% for threonine, and 81% for tyrosine. Our computational experiments show significant improvement in the performance of prediction relative to a single feature, or to the combined feature with equal weights. Moreover, our systematic integration method significantly improves the prediction preformance compared with the previous well-known methods.

• Journal of the Korean Magnetic Resonance Society
• /
• v.12 no.2
• /
• pp.65-73
• /
• 2008

HP1298 (Swiss-Prot ID ; P65108) is an 72-residue protein from Helicobacter pylori strain 26695. The function of HP1298 was identified as Translation initiation factor IF-l based on sequence homology, and HP1298 is included in IF-l family. Here, we report the sequence-specific backbone resonance assignments of HP1298. About 97% of all the $^{1}HN$, $^{15}N$, $^{13}C{\alpha}$, $^{13}C{\beta}$, and $^{13}CO$ resonances could be assigned unambiguously. We could predict the secondary structure of HP1298, by analyzing the deviation of the $^{13}C{\alpha}$ and $^{13}C{\beta}$ shemical shifts from their respective random coil values. Secondary structure prediction shows that HP1298 consists of six $\beta$-strands. This study is a prerequisite for determining the solution structure of HP1298 and investigating the structure-function relationship of HP1298. Assigned chemical shift can be used for the study on interaction between HP1298 and other Helicobacter pylori proteins.

• Journal of Microbiology and Biotechnology
• /
• v.28 no.3
• /
• pp.454-464
• /
• 2018

Salivary microbiota alterations can correlate with dental caries development in children, and mechanisms mediating this association need to be studied in further detail. Our study explored salivary microbiota shifts in children and their association with the incidence of dental caries with dentine involvement. Salivary samples were collected from children with caries and their subsequently matched caries-free controls before and after caries development. The microbiota was analyzed by 16S rRNA gene-based high-throughput sequencing. The salivary microbiota was more diverse in caries-free subjects than in those with dental caries with dentine involvement (DC). Although both groups exhibited similar shifts in microbiota composition, an association with caries was found by function prediction. Analysis of potential microbiome functions revealed that Granulicatella, Streptococcus, Bulleidia, and Staphylococcus in the DC group could be associated with the bacterial invasion of epithelial cells, phosphotransferase system, and ${\text\tiny{D}}-alanine$ metabolism, whereas Neisseria, Lautropia, and Leptotrichia in caries-free subjects could be associated with bacterial motility protein genes, linoleic acid metabolism, and flavonoid biosynthesis, suggesting that functional differences in the salivary microbiota may be associated with caries formation. These results expand the current understanding of the functional significance of the salivary microbiome in caries development, and may facilitate the identification of novel biomarkers and treatment targets.

• Proceedings of the Korea Information Processing Society Conference
• /
• 2008.05a
• /
• pp.431-432
• /
• 2008

정보처리 기술의 발전에 따라 정보기술을 통한 생명과학 문제 해결을 연구하는 생명정보학(bioinformatics) 분야에서도 보다 대용량의 바이오 정보를 처리하게 되었다. 특히 우리 몸을 이루는 핵심 요소인 단백질의 기능 예측 자동화는 다루어야 할 정보량이 매우 방대한 관계로 일찍부터 컴퓨터를 사용한 정보처리 기법이 중요하게 다루어져 왔다. 본 연구에서는 특정 단백질 주변의 미세환경 (microenvironment)에 관한 정보를 수집하고 분석하여 그 기능이 알려진 다른 종류의 단백질 주변의 미세환경과 비교함으로써 기능을 예측하는 방법에 대해 소개한다.

• Genomics & Informatics
• /
• v.13 no.2
• /
• pp.53-59
• /
• 2015

In developing countries threat of cholera is a significant health concern whenever water purification and sewage disposal systems are inadequate. Vibrio cholerae is one of the responsible bacteria involved in cholera disease. The complete genome sequence of V. cholerae deciphers the presence of various genes and hypothetical proteins whose function are not yet understood. Hence analyzing and annotating the structure and function of hypothetical proteins is important for understanding the V. cholerae. V. cholerae O139 is the most common and pathogenic bacterial strain among various V. cholerae strains. In this study sequence of six hypothetical proteins of V. cholerae O139 has been annotated from NCBI. Various computational tools and databases have been used to determine domain family, protein-protein interaction, solubility of protein, ligand binding sites etc. The three dimensional structure of two proteins were modeled and their ligand binding sites were identified. We have found domains and families of only one protein. The analysis revealed that these proteins might have antibiotic resistance activity, DNA breaking-rejoining activity, integrase enzyme activity, restriction endonuclease, etc. Structural prediction of these proteins and detection of binding sites from this study would indicate a potential target aiding docking studies for therapeutic designing against cholera.

• Journal of the Korean Institute of Intelligent Systems
• /
• v.19 no.5
• /
• pp.730-736
• /
• 2009

It is more important to analysis of huge gemonics data in Bioinformatics. Here we present a novel datamining approach to predict structure and function using protein's primnary structure only. We propose not also to develope n-Block substring search algorithm in reducing enormous search space effectively in relation to feature selection, but to formulate weighted linear algorithm in a prediction of structure and function of a protein using primary structure. And we show efficient in protein domain characterization and classification by calculation weight value in determining domain association in each selected substring, and also reveal that more efficient results are acquired through claculated model score result in an inference about degree of association with each CDS(coding sequence) in domain.

• Bulletin of the Korean Chemical Society
• /
• v.31 no.5
• /
• pp.1247-1251
• /
• 2010

We propose an improved solvent contact model to estimate the solvation free energies of amino acids from individual atomic contributions. The modification of the solvation model involves the optimization of three kinds of parameters in the solvation free energy function: atomic fragmental volume, maximum atomic occupancy, and atomic solvation parameters. All of these atomic parameters for 17 atom types are developed by the operation of a standard genetic algorithm in such a way to minimize the difference between experimental and calculated solvation free energies. The present solvation model is able to predict the experimental solvation free energies of amino acids with the squared correlation coefficients of 0.94 and 0.93 for the parameterization with Gaussian and screened Coulomb potential as the envelope functions, respectively. This result indicates that the improved solvent contact model with the newly developed atomic parameters would be a useful tool for the estimation of the molecular solvation free energy of a protein in aqueous solution.

• Macromolecular Research
• /
• v.14 no.6
• /
• pp.654-658
• /
• 2006

Recent developments in equations of state for molecular fluids have demonstrated the feasibility of using the hard-sphere equation to describe the effects of repulsive forces in simple fluids. By including a suitable term for attractive forces, most conveniently a uniform background potential, the properties of bio-macromolecular interaction can be roughly calculated. However, the choice of the potential used in perturbed hard-sphere chain (PHSC) theory for describing the attractions between macromolecules is rather complicated. For hard-sphere chains, the prediction accuracy from each model strongly depends on the choice of potential function.