• 한국생물정보학회:학술대회논문집
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• 한국생물정보시스템생물학회 2000년도 International Symposium on Bioinformatics
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• pp.28-31
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• 2000

We describe a hidden Markov model, HMMTIR, for general protein sequence based on the I-sites library of sequence-structure motifs. Unlike the linear HMMs used to model individual protein families, HMMSTR has a highly branched topology and captures recurrent local features of protein sequences and structures that transcend protein family boundaries. The model extends the I-sites library by describing the adjacencies of different sequence-structure motifs as observed in the database, and achieves a great reduction in parameters by representing overlapping motifs in a much more compact form. The HMM attributes a considerably higher probability to coding sequence than does an equivalent dipeptide model, predicts secondary structure with an accuracy of 74.6% and backbone torsion angles better than any previously reported method, and predicts the structural context of beta strands and turns with an accuracy that should be useful for tertiary structure prediction. HMMSTR has been incorporated into a public, fully-automated protein structure prediction server.

• 한국자기공명학회논문지
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• 제17권1호
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• pp.59-66
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• 2013

BldD, a developmental transcription factor from Streptomyces coelicolor, is a homodimeric, DNA-binding protein with 167 amino acids in each subunit. Each monomer consists of two structurally distinct domains, the N-terminal domain (BldD-NTD) responsible for DNA-binding and dimerization and the C-terminal domain (BldD-CTD). In contrast to the BldD-NTD, of which crystal structure has been solved, the BldD-CTD has been characterized neither in structure nor in function. Thus, in terms of structural genomics, structural study of the BldD-CTD has been conducted in solution, and in the present work, mainchain NMR assignments of the recombinant BldD-CTD (residues 80-167 of BldD) could be achieved by a series of heteronuclear multidimensional NMR experiments on a [$^{13}C/^{15}N$]-enriched protein sample. Finally, the secondary structure prediction by CSI and TALOS+ analysis using the assigned chemical shifts data identified a ${\beta}-{\alpha}-{\alpha}-{\beta}-{\alpha}-{\alpha}-{\alpha}$ topology of the domain. The results will provide the most fundamental data for more detailed approach to the atomic structure of the BldD-CTD, which would be essential for entire understanding of the molecular function of BldD.

• Genomics & Informatics
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• 제21권2호
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• pp.25.1-25.12
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• 2023

Adaptation of infections and hosts has resulted in several metabolic mechanisms adopted by intracellular pathogens to combat the defense responses and the lack of fuel during infection. Human tuberculosis caused by Mycobacterium tuberculosis (MTB) is the world's first cause of mortality tied to a single disease. This study aims to characterize and anticipate potential antigen characteristics for promising vaccine candidates for the hypothetical protein of MTB through computational strategies. The protein is associated with the catalyzation of dithiol oxidation and/or disulfide reduction because of the protein's anticipated disulfide oxidoreductase properties. This investigation analyzed the protein's physicochemical characteristics, protein-protein interactions, subcellular locations, anticipated active sites, secondary and tertiary structures, allergenicity, antigenicity, and toxicity properties. The protein has significant active amino acid residues with no allergenicity, elevated antigenicity, and no toxicity.

• 한국정보통신학회논문지
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• 제22권1호
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• pp.26-32
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• 2018

단백질의 이차구조는 단백질의 진화, 구조, 기능을 연구하는데 중요한 정보이다. 단백질 서열 정보만을 이용하여 단백질의 이차 구조를 예측하는 분야에 심층 학습 방법들이 최근 들어 활발히 적용되고 있다. 이러한 방법에서 널리 사용되는 입력은 단백질 서열을 변환하여 만들어진 단백질 프로파일이다. 본 논문에서는 효과적인 단백질 프로파일을 얻기 위하여 단백질 서열 탐색 방법으로 PSI-BLAST와 더불어서 HHblits를 사용하였다. 단백질 프로파일의 구성에 사용되는 상동 단백질 서열을 결정하기 위한 유사도 문턱치와 상동 단백질 서열 정보를 반복적으로 사용하는 회수를 조절하였다. 합성곱 신경망과 순환 신경망을 사용하여 단백질 이차구조를 예측하였는데, 진화적 정보를 한번만 추가하여 만들어진 단백질 프로파일이 효과적이었다.

• 한국자기공명학회논문지
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• 제13권2호
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• pp.117-125
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• 2009

HP0062 is an 86 residue hypothetical protein from Helicobacter pylori strain 26695. HP0062 was identified ESAT-6/WXG100 superfamily protein based on structure and sequence alignment and also contains leucine zipper domain sequence. Here, we report the sequence-specific backbone resonance assignment of HP0062. About 97.7% of all $^1H_N,\;^{15}N,\;^{13}C_{\alpha},\;^{13}C_{\beta}\;and\;^{13}C=O$ resonances were assigned unambiguously. We could predict the secondary structure of HP0062 by analyzing the deviation of the $^{13}C_{alpha}\;and\;^{13}C_{\beta}$ chemical shifts from their respective random coil values. Secondary structure prediction shows that HP0062 consist of two ${\alpha}$-helices. This study is a prerequisite for determining the solution structure of HP0062 and can be used for the study on interaction between HP0062 and DNA and other Helicobacter pylori proteins.

• 한국자기공명학회논문지
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• 제12권2호
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• pp.65-73
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• 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.

• 한국자기공명학회논문지
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• 제11권2호
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• pp.73-84
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• 2007

MTH1821 (UniProtKB/TrEMBL ID O27849) is a 96-residue hypothetical protein from the open reading frame of Methanobacterium thermoautotrophicum H one of the target organisms of structural genomics pilot project. Proteins which contain conserved sequence compared with MTH1821 have not been discovered yet and the functional and structural information for MTH1821 is not available. Here, we present the sequence-specific backbone resonance using multidimensional heteronuc1ear NMR spectroscopy and propose the secondary structure using GetSBY software. The backbone resonances of N, HN, $C_{\alpha}$, $C_{\beta}$, CO and $H_{\alpha}$ which are necessary for a prediction of secondary structure by GetSBY were assigned about 98% (557/568). The secondary structure of MTH1821 confirmed that it is comprised of four strand regions and two helical regions. This report will provide a valuable resource for the calculation solution structure of MTH1821 and for the other hypothetical protein that is targeted for structural-based functional discovery.

• 한국자기공명학회논문지
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• 제15권1호
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• pp.69-79
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• 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.

• 한국생물정보학회:학술대회논문집
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• 한국생물정보시스템생물학회 2003년도 제2차 연례학술대회 발표논문집
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• pp.268-274
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• 2003

Most currently known molecular structures were determined by X-ray crystallography or Nuclear Magnetic Resonance (NMR). These methods generate a large amount of structure data, even far small molecules, and consist mainly of three-dimensional atomic coordinates. These are useful for analyzing molecular structure, but structure elements at higher level are also needed for a complete understanding of structure, and especially for structure prediction. Computational approaches exist for identifying secondary structural elements in proteins from atomic coordinates. However, similar methods have not been developed for RNA due in part to the very small amount of structure data so far available, and extracting the structural elements of RNA requires substantial manual work. Since the number of three-dimensional RNA structures is increasing, a more systematic and automated method is needed. We have developed a set of algorithms for recognizing secondary and tertiary structural elements in RNA molecules and in the protein-RNA structures in protein data banks (PDB). The present work represents the first attempt at extracting RNA structure elements from atomic coordinates in structure databases. The regularities in the structure elements revealed by the algorithms should provide useful information for predicting the structure of RNA molecules bound to proteins.

• 한국자기공명학회논문지
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• 제19권1호
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• pp.49-53
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• 2015

MRA1997 is a 76-residue conserved hypothetical protein of Mycobacterium tuberculosis H37Ra, one of the most pathogenic bacterial species and the causative agent of tuberculosis. In this study, the sequence-specific backbone resonance assignment of MRA1997 was performed using NMR spectroscopy. Approximately 88.3% of the total resonances could be unambiguously assigned. By analyzing deviations of the $C{\alpha}$ and $C{\beta}$ chemical shift values, the secondary structure of MRA1997 was calculated. The result revealed that secondary structure of MRA 1997 consists of one ${\alpha}$-helix and five ${\beta}$-sheets. Our structural study will be a footstone towards the characterization of the three-dimensional structure of MRA1997.