• 제목/요약/키워드: Secondary structure of proteins

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Backbone 1H, 15N, and 13C Resonance Assignments and Secondary-Structure of the Conserved Hypothetical Protein HP0892 of Helicobacter pylori

  • Han, Kyung-Doo;Park, Sung-Jean;Jang, Sun-Bok;Lee, Bong-Jin
    • Molecules and Cells
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    • 제25권1호
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    • pp.138-141
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    • 2008
  • HP0892 (SwissProt/TrEMBL ID O25552) is a 90-residue conserved hypothetical protein from Helicobacter pylori strain 26695, with a calculated pI of 9.38 and a molecular mass of 10.41 kDa. It belongs to the Plasmid stabilization system protein family (PF05016) in the Pfam database. Proteins with sequence similarity to HP0892 exist in Vibrio choierae, Enterococcus faecalis, Campylobacter jejuni, Streptococcus pneumoniae, Haemophilus influenzae, Escherichia coli O157. Here we report the sequence-specific backbone resonance assignments of HP0892 using multidimentional heteronuclear NMR spectroscopy. About 97.0% (422/435) of the HN, N, CO, $C{\beta}$, $C{\alpha}$ resonances of 90 residues of HP0892 were assigned. On the basis of the resonance assignments, three helical regions and four strand regions were identified using the CSI program. This study is a prerequisite for calculating the solution structure of HP0892, and will be useful for studying its interaction with other molecules.

Structural Properties of Fibril-forming Segments of α-Synuclein

  • Yoon, Je-Seong;Park, Joon-Ho;Jang, Soon-Min;Lee, Kyung-Hee;Shin, Seo-Min
    • Bulletin of the Korean Chemical Society
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    • 제30권3호
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    • pp.623-629
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    • 2009
  • We have performed replica-exchange molecular dynamics simulations on 41 residue peptide mainly composed of NAC (non A$\beta$ component) sequence in $\alpha$-Synuclein. To investigate conformational characteristics of intrinsically unstructured peptides, we carried out structural analysis on the ‘representative structures’ for ensemble of structures occurring at different temperatures. The secondary structure profile obtained from our simulations suggests that the NAC region of $\alpha$-synuclein can be divided into roughly three helical-like segments. It is found that the overall helix-turn-helix like topology is conserved even though the conformational fluctuations grow as the temperature increases. The coordinate-based and the distance-based representative structures exhibit noticeable differences at higher temperatures while they are similar at lower temperatures. It is found that structural variations for the coordinate-based representative structures are much larger, suggesting that distance-based representative structures provide more reliable information concerning characteristic features of intrinsically unstructured proteins. The present analysis also indicates that the conformational features of representative structures at high temperatures might be related to those in membrane or low pH environment.

온도변화에 의한 cAMP 수용성 단백질(CRP)의 구조 (Study on the structure of cAMP receptor protein(CRP) by temperature change)

  • 주종호;구미자;강종백
    • 생명과학회지
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    • 제10권3호
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    • pp.279-285
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    • 2000
  • cAMP 수용성 단백질인 CRP는 Escherichia coli에서 대사와 관련된 유전자의 전사를 조절한다. 본 연구는 야생형과 돌연변이 CRP 단백질의 열적 안정성과 온도에 따른 단백질의 구조변화를 관찰하기 위 하여 proteolytic digestion, UV spectrophotometer, CD spectrapolarimeter 등의 방법을 사용하였다. cAMP가 없을 때에는 야생형, S83G, S128A CRP가 열적 안정성에서 큰 차이를 보이지 않았지만, cAMP가 존재할 때 야생형 CRP가 다른 돌연변이 CRP보다 열적으로 더욱 안정함을 보였다. 그리고 protease digestion 실험을 통하여 높은 온도에서 cAMP의 존재와 무관하게 돌연변이 CRP에서 단백질 의 변성으로 인한 절단된 단백질띠를 관찰할 수 있었다. 그리고 55$^{\circ}C$에서 측정한 CD 스펙트럼에서 단백 질의 2차 구조인 $\alpha$-helix 구조가 부분적으로 파괴되었음이 관찰되었다.

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The SL1 Stem-Loop Structure at the 5′-End of Potato virus X RNA Is Required for Efficient Binding to Host Proteins and forViral Infectivity

  • Kwon, Sun-Jung;Kim, Kook-Hyung
    • Molecules and Cells
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    • 제21권1호
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    • pp.63-75
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    • 2006
  • The 5′-region of Potato virus X (PVX) RNA, which contains an AC-rich, single-stranded region and stem-loop structure 1 (SL1), affects RNA replication and assembly. Using Systemic Evolution of Ligands by EXponential enrichment (SELEX) and the electrophoretic mobility shift assay, we demonstrate that SL1 interacts specifically with tobacco protoplast protein extracts (S100). The 36 nucleotides that correspond to the top region of SL1, which comprises stem C, loop C, stem D, and the tetra loop (TL), were randomized and bound to the S100. Remarkably, the wild-type (wt) sequence was selected in the second round, and the number of wt sequences increased as selection proceeded. All of the selected clones from the fifth round contained the wt sequence. Secondary structure predictions (mFOLD) of the recovered sequences revealed relatively stable stem-loop structures that resembled SL1, although the nucleotide sequences therein were different. Moreover, many of the clones selected in the fourth round conserved the TL and C-C mismatch, which suggests the importance of these elements in host protein binding. The SELEX clone that closely resembled the wt SL1 structure with the TL and C-C mismatch was able to replicate and cause systemic symptoms in plants, while most of the other winners replicated poorly only on inoculated leaves. The RNA replication level on protoplasts was also similarly affected. Taken together, these results indicate that the SL1 of PVX interacts with host protein(s) that play important roles related to virus replication.

Homology Modeling and Molecular Docking Study of Translationally Controlled Tumor Protein and Artemisinin

  • Chae, Jin-Sun;Choi, In-Hee;Kim, Choon-Mi
    • Archives of Pharmacal Research
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    • 제29권1호
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    • pp.50-58
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    • 2006
  • Translationally controlled tumor protein (TCTP), also known as histamine releasing factor (HRF), is found abundantly in different eukaryotic cell types. The sequence homology of TCTP between different species is very high, belonging to the MSS4/DSS4 superfamily of proteins. TCTP is involved in both cell growth and human late allergy reaction, as well as having a calcium binding property; however, its primary biological functions remain to be clearly elucidated. In regard to many possible functions, the TCTP of Plasmodium falciparum (Pf) is known to bind with an antimalarial agent, artemisinin, which is activated by heme. It is assumed that the endoperoxide-bridge of artemisinin is opened up by heme to form a free radical, which then eventually alkylates, probably to the Cys14 of PfTCTP. Study of the docking of artemisinin with heme, and subsequently with PfTCTP, was carried out to verify the above hypothesis on the basis of structural interactions. The three dimensional (3D) structure of PfTCTP was built by homology modeling, using the NMR structure of the TCTP of Schizosaccharomyces pombe as a template. The quality of the model was examined based on its secondary structure and biological function, as well as with the use of structure evaluating programs. The interactions between artemisinin, heme and PfTCTP were then studied using the docking program, FlexiDock. The center of the peroxide bond of artemisinin and the Fe of heme were docked within a short distance of $2.6{\AA}$, implying the strong possibility of an interaction between the two molecules, as proposed. When the activated form of artemisinin was docked on the PfTCTP, the C4-radical of the drug faced towards the sulfur of Cys14 within a distance of $2.48{\AA}$, again suggesting the possibility of alkylation having occurred. These results confirm the proposed mechanism of the antimalarial effect of artemisinin, which will provide a reliable method for establishing the mechanism of its biological activity using a molecular modeling study.

Differences in pork myosin solubility and structure with various chloride salts and their property of pork gel

  • Hyun Gyung Jeong;Jake Kim;Seonmin Lee;Kyung Jo;Hae In Yong;Yun-Sang Choi;Samooel Jung
    • Journal of Animal Science and Technology
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    • 제65권5호
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    • pp.1065-1080
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    • 2023
  • The solubility and structure of myosin and the properties of pork gel with NaCl, KCl, CaCl2, and MgCl2 were investigated. Myofibrillar proteins (MPs) with phosphate were more solubilized with NaCl than with KCl (p < 0.05). CaCl2 and MgCl2 showed lower MP solubilities than those of NaCl and KCl (p < 0.05). The α-helix content of myosin was lower in KCl, CaCl2, and MgCl2 than in NaCl (p < 0.05). The pH of pork batter decreased in the order of KCl, NaCl, MgCl2, and CaCl2 (p < 0.05). The cooking yield of the pork gel manufactured with monovalent salts was higher than that of the pork gel manufactured with divalent salts (p < 0.05). The pork gel manufactured with KCl and MgCl2 showed lower hardness than that of the pork gel manufactured with NaCl. The solubility and structure of myosin were different with the different chloride salts and those led the different quality properties of pork gel. Therefore, the results of this study can be helpful for understanding the quality properties of low-slat meat products manufactured by replacing sodium chloride with different chloride salts.

Comparative Genomics of T-complex protein 10 like in Humans and Chimpanzees

  • Kim, Il-Chul;Kim, Dae-Soo;Kim, Dae-Won;Choi, Sang-Haeng;Choi, Han-Ho;Chae, Sung-Hwa;Park, Hong-Seog
    • Genomics & Informatics
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    • 제3권2호
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    • pp.61-65
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    • 2005
  • Comparing 231 genes on chimpanzee chromosome 22 with their orthologous on human chromosome 21, we have found that 15 orthologs have indels within their coding sequences. It was rather surprising that significant number of genes have changed by indel, despite the shorter time since their divergence and led us hypothesize that indels and structural changes may represent one of the major mechanism of proteome evolution in the higher primates. Human T-complex protein 10 like (TCP 10L) is a representative having indel within its coding sequence. Gene structure of human TCP10L compared with chimpanzee TCP10L gene showed 16 base pair difference in genomic DNA. As a result of the indel, frame shift mutation occurs in coding sequence (CDS) and human TCP10L express longer polypeptide of 21 amino acid residues than that of chimpanzee. Our prediction found that the indel may affect to dramatic change of secondary protein structure between human and chimpanzee TCP10L. Especially, the structural changes in the C-terminal region of TCP10L protein may affect on the interacting potential to other proteins rather than DNA binding function of the protein. Through these changes, TCP10L might influence gene expression profiles in liver and testis and subsequently influence the physiological changes required in primate evolution.

대장균 트립토판 중합효소 α 소단위체의 응집 형성에 미치는 잔기 173 치환체의 억제 효과 (Suppression of a Residue 173 Mutant Form on Aggregation of Tryptophan Synthase α-Subunits from Escherichia coli)

  • 정재갑;박후휘;임운기
    • 생명과학회지
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    • 제32권9호
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    • pp.729-733
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    • 2022
  • 수용성 단백질이 비정상적인 불용성 응집(aggregate)으로 전환되면 질환 등 여러 문제를 야기된다. 대장균 트립토판 중합효소 α 소단위체(αTS)는 가장 흔한 구조의 하나인 TIM 배럴 구조를 가지고 있다. 이전의 연구에서 불용성 응집이 일어나는 여러 잔기치환체(Y4C, S33L, P28L, P28S, G44S, D46N, P96L, P96S)를 얻었다. 본 연구에서는 높은 안정성과 도메인 협동성 성질을 보여주는 Y173F가 다른 잔기자리에 치환으로 유도된 응집 형성을 억제할 수 있는 지 여부를 조사했다. 8개 모두에서 억제효과를 보여 주었다. 단백질 분리가 가능한 P28L αTS를 분석한 결과, 이차구조함량의 감소, 안정성 감소, 소수성표면 증가 등의 구조변화특성을 보여주었다. Y173F가 첨가된 P28L/Y173F αTS은 야생형과 비슷한 구조로 회복되었다. 본 연구는 소수성 코아에 위치하는 Tyr173 잔기처럼 응집을 유도하는 여러 다른 잔기 자리를 보편적으로 억제하는 잔기가 존재할 수 있음을 시사해 준다.

Physical, Chemical Properties and Structural Changes of Zaodan Pickled by Vacuum Decompression Technology

  • Sun, Naxin;Liu, Huiping;Zhang, Xiaowei;Wang, Hongni;Liu, Shaojuan;Chen, Pei;Yu, Weijie;Liu, Kai
    • 한국축산식품학회지
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    • 제38권2호
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    • pp.291-301
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    • 2018
  • To shorten the production cycle of Zaodan, this study first pickled Zaodan by a novel technology - vacuum decompression technology. Vacuum decompression technology could reduce the pickling time of Zaodan from 20 wk to about 9 wk. The protein content, moisture and pH of the Zaodan egg white gradually decreased with a concomitant increase in salt during the pickling process. The total sulfhydryl group (SH) group content of the egg white proteins was increased to $2.43{\times}10^{-3}mol/L$ after being pickled for 30 d, whereas the content of disulphide bonds (SS) was reduced to $23.35{\times}10^{-3}mol/L$. The surface hydrophobicity was lowest after pickling for 30 d. In addition, great changes occurred in the secondary structure of the egg white proteins after pickling for 20 d. The disappearance of ovomucin was noticeable based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis.

단백질 구조 예측을 위한 서열 연관 규칙 탐사 (Discovering Sequence Association Rules for Protein Structure Prediction)

  • 김정자;이도헌;백윤주
    • 정보처리학회논문지D
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    • 제8D권5호
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    • pp.553-560
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    • 2001
  • 바이오정보학(bioinformatic)은 생물학 분야 특히 분자 수준의 유전체 연구에서 발생하는 데이터를 저장, 관리, 분석하여 실험 프로젝트를 지원함은 물론, 기능 예측 및 조절에 대한 실험 설계를 가능하게 하는 제반 컴퓨터 기술을 의미한다. 유전체 연구의 다양한 접근 방식 중 단백체학(proteomics)는 유전체의 최종 산물인 단백질을 직접적으로 다룬다는 측면에서 그 효용성에 대해 많은 기대를 모으고 있다. 본 논문에서는 단백질의 기능을 결정하는 가장 중요한 요소 중 하나인 단백질의 구조를 예측하기 위한 데이터 마이닝 기법을 제안한다. 단백질의 일차 구조인 아미노산 서열에 타나나는 부서열간의 연관성이 해당 단백질의 이차 혹은 삼차 구조를 결정하는 중요한 단서임을 설명하고, 아미노산 부서열간의 연관성을 표현하기 위한 모델로서 서열 연관 규직을 정의한다. 서열 연관 규칙의 유용성을 평가하기 위한 지지도와 신뢰도를 새롭게 정의하고, 주어진 단백질 집단으로부터 유용한 서열 연관 규칙을 발견하기 위한 기법을 제안한다. 아울러, SWISS-PROT 단백질 데이터베이스로부터 입수한 단백질 서열 데이터를 이용하여 제안한 기법의 성능을 평가한다.

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