• 제목/요약/키워드: protein structure

검색결과 1,715건 처리시간 0.044초

In-cell nuclear magnetic resonance spectroscopy for studying intermolecular interactions

  • Sugiki, Toshihiko;Lin, Yuxi;Lee, Young-Ho
    • 한국자기공명학회논문지
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    • 제23권1호
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    • pp.33-39
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    • 2019
  • Studies on the interactions of proteins with partner molecules at the atomic resolution are essential for understanding the biological function of proteins in cells and for developing drug molecules. Solution NMR spectroscopy has shown remarkably useful capability for investigating properties on the weak to strong intermolecular interactions in both diluted and crowded solution such as cell lysates. Of note, the state-of-the-art in-cell NMR method has made it possible to obtain atomistic information on natures of intermolecular interactions between target proteins with partner molecules in living cells. In this mini-review, we comprehensively describe the several technological advances and developments in the in-cell NMR spectroscopy.

자외선 조사가 Ovalbumin의 분자적 성질에 미치는 영향 (Effect of Ultraviolet Irradiation on Molecular Properties of Ovalbumin)

  • 조용식;송경빈;산전경로;한귀정
    • Applied Biological Chemistry
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    • 제51권4호
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    • pp.276-280
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    • 2008
  • 식품 allergen 저감화 수단으로 자외선 조사의 타당성을 검토하고 자외선조사가 식품 단백질의 분자적 성질에 미치는 영향을 조사하고자 ovalbumin 용액에 자외선을 조사한 후 단백질의 분자량 분포와 2차구조 및 3차구조의 변화를 조사하였다. SDS-PAGE와 Gel permeation chromatography 결과 ovalbumin은 자외선 조사에 의하여 단백질이 분해되고 조사시간이 증가할수록 펩티드가 중합하는 형태를 나타냈다. Circular dichroism 연구는 자외선 조사에 의하여 ${\alpha}$-helix 구조가 감소하고 조사시간이 증가할 경우 compact denatured ovalbumin의 구조를 나타내는 2차구조의 변화를 나타냈다. 자외선 조사된 ovalbumin의 형광스펙트럼은 조사시간이 증가할수록 단백질의 maximum emission intensity가 감소하는 3차구조의 변화를 나타냈다. 결과적으로 자외선 조사는 ovalbumin의 분자적 성질을 변화시키며 allergen의 항원성을 변화시키는 수단으로 이용가능성을 시사한다.

국내에서 분리된 일본뇌염 바이러스의 Envelope Protein의 3차구조 분석 (Analysis of the Three Dimensional Structure of Envelope Protein of the Japanes encephalitis virus Isolated in Korea)

  • 남재환;채수림;김은정;윤경식;이호동;고현철;조해월
    • 대한바이러스학회지
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    • 제27권2호
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    • pp.209-216
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    • 1997
  • Three dimensional structures of envelope protein from Korean isolates and Nakayama-NIH strain of Japanese encephalitis virus (JEV) were deduced by a computer program (HyperChem 4.0 Chemplus 1.0) based on the data of the three dimentional structure of Tick-borne encephalitis virus. In the three dimensional structure of envelope protein, neutralizing epitope and T-helper cell recognition site of C-terminal region of Korean isolates were structually similar to those of Nakayama-NIH but the N-terminal region was not. Korean JE isolates were compared with Nakayama-NIH strain by using cross-neutralization antibody test. Neutralizing activities of Korean isolates derived from guinea pigs were higher than those of Nakayama-NIH strain against Korean isolates, although the polyclonal antibody titers of Nakayama-NlH showed 1:160 to 1:640 against Korean isolates. According to the results from three dimentional structures and cross-neutralization analyses, the antigenic difference between Korean JE isolates and Nakayama-NIH strain may be dependent on structural difference of envelope protein.

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인산화와 초산화가 대두단백질의 기능특성과 구조에 미치는 영향 (Effects of Phosphorylation and Acetylation on Functional Properties and Structure of Soy Protein)

  • 김남수;권대영;남영중
    • 한국식품과학회지
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    • 제20권5호
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    • pp.625-630
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    • 1988
  • 대두단백질을 인산화 및 초산화처리에 의하여 변형시키고, 변형대두단백질의 기능특성을 검토하였다. 인산화 대두단백질은 비변형 대두단백질보다 높은, 용해도, 거품특성, 수분보유력을 나타냈다. 한편, 초산화에 의해서도 유화력과 거품특성이 현저하게 증진되었다. 대두단백질은 인산화와 초산화에 의하여 등전점이 산성쪽으로 변화였으며 단백질의 집괴화현상도 관찰되었다. 또한, 화학변형된 대두단백질을 디스크 전기영동에 의해 분석시 단백질밴드의 상대이동도가 현저하게 증대되었다.

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Mutational Analysis of an Essential RNA Stem-loop Structure in a Minimal RNA Substrate Specifically Cleaved by Leishmania RNA Virus 1-4 (LRV1-4) Capsid Endoribonuclease

  • Ro, Youngtae;Patterson, Jean L.
    • Journal of Microbiology
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    • 제41권3호
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    • pp.239-247
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    • 2003
  • The LRV1-4 capsid protein possesses an endoribonuclease activity that is responsible for the single site-specific cleavage in the 5' untranslated region (UTR) of its own viral RNA genome and the formation of a conserved stem-loop structure (stem-loop IV) in the UTR is essential for the accurate RNA cleavage by the capsid protein. To delineate the nucleotide sequences, which are essential for the correct formation of the stem-loop structure for the accurate RNA cleavage by the viral capsid protein, a wildtype minimal RNA transcript (RNA 5' 249-342) and several synthetic RNA transcripts encoding point-mutations in the stem-loop region were generated in an in vitro transcription system, and used as substrates for the RNA cleavage assay and RNase mapping studies. When the RNA 5' 249-342 transcript was subjected to RNase T1 and A mapping studies, the results showed that the predicted RNA secondary structure in the stem-loop region using FOLD analysis only existed in the presence of Mg$\^$2+/ ions, suggesting that the metal ion stabilizes the stem-loop structure of the substrate RNA in solution. When point-mutated RNA substrates were used in the RNA cleavage assay and RNase T1 mapping study, the specific nucleotide sequences in the stem-loop region were not required for the accurate RNA cleavage by the viral capsid protein, but the formation of a stem-loop like structure in a region (nucleotides from 267 to 287) stabilized by Mg$\^$2+/ ions was critical for the accurate RNA cleavage. The RNase T1 mapping and EMSA studies revealed that the Ca$\^$2+/ and Mn$\^$2+/ ions, among the reagents tested, could change the mobility of the substrate RNA 5' 249-342 on a gel similarly to that of Mg$\^$2+/ ions, but only Ca$\^$2+/ ions identically showed the stabilizing effect of Mg$\^$2+/ ions on the stem-loop structure, suggesting that binding of the metal ions (Mg$\^$2+/ or Ca$\^$2+/) onto the RNA substrate in solution causes change and stabilization of the RNA stem-loop structure, and only the substrate RNA with a rigid stem-loop structure in the essential region can be accurately cleaved by the LRV1-4 viral capsid protein.

RBF정제단백질의 핵산결합도 및 PKR효소의 인산화억제효과의 비교에 관한 연구 (Comparative Study of Nucletic Acid Binding of the Purified RBF Protein and Its Inhibition of PKR phosphorylation)

  • 박희성;김인수
    • 생명과학회지
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    • 제8권2호
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    • pp.119-125
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    • 1998
  • dsRNA결합인자인 RBF단백질을 정제하여 이의 단일 또는 이중선의 RNA 또는 DNA 와의 결합도를 측정하였다ㅓ. RBF단백질은 이들과 각각 반응시켜 그 결합도는 SDS-PAGE에 의하여 비교관찰하였다. RBF단백질은 dsRNA와은 강한 결합력을 나타낸 반면 기타의 핵산구조에 대해서는 이러한 결과를 나타내지 못하였다. 인산화 실험의 결과, RBF단백질은 poly(I) : poly(C)의 존재하에서 사람 도는 쥐 모두로 부터의 PKR 효소의 자가인산화를 유사한 방식으로 억제하였다. 이는 다른 종류의 진핵세포생물에서 단백질합성조절을 위한 PKR과 RBF가 유사한 경쟁적 관련성을 유지하면서 존재함을 시사하고 있다.

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클러스터 세그먼트 인덱스를 이용한 단백질 이차 구조의 효율적인 유사 검색 (Clustered Segment Index for Efficient Approximate Searching on the Secondary Structure of Protein Sequences)

  • 서민구;박상현;원정임
    • 한국정보과학회논문지:데이타베이스
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    • 제33권3호
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    • pp.251-260
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    • 2006
  • 단백질 일차 구조(아미노산 배열)에 대한 상동 검색은 유전자나 단백질의 기능과 진화 과정을 유추하기 위한 필수 연산이다. 그러나 진화 단계가 멀리 떨어진 경우 단백질 일차 구조는 보존되지 않기 때문에 단백질의 공간적 구조에 대한 유사 검색을 통해서만 진화 단계를 유추할 수 있다. 따라서 본 논문에서는 단백질의 공간적 구조를 표현하는 단백질 이차 구조를 대상으로 하여 RDBMS상에 쉽게 구현이 가능한 인덱싱 방안을 제안한다. 제안된 인덱싱 방안은 클러스터링 기법과 LookAhead 개념을 활용하여 Exact Match, Range Match, Wildcard Match 질의를 신속하게 처리한다. 제안된 방법의 우수성을 검증하기 위하여 실제의 단백질 데이타를 대상으로 성능 평가를 수행하였다. 실험 결과에 의하면, 제안된 방법은 기존의 방법과 비교하여 Exact Match의 경우 6.3배까지, Range Match의 경우 3.3배까지, Wildcard Match의 경우 1.5배까지의 개선된 검색 성능을 가지는 것으로 나타났다.

Backbone 1H, 15N, and 13C Resonance Assignment and Secondary Structure Prediction of HP0495 from Helicobacter pylori

  • Seo, Min-Duk;Park, Sung-Jean;Kim, Hyun-Jung;Seok, Seung-Hyeon;Lee, Bong-Jin
    • BMB Reports
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    • 제40권5호
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    • pp.839-843
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    • 2007
  • HP0495 (Swiss-Prot ID; Y495_HELPY) is an 86-residue hypothetical protein from Helicobacter pylori strain 26695. The function of HP0495 cannot be identified based on sequence homology, and HP0495 is included in a fairly unique sequence family. Here, we report the sequencespecific backbone resonance assignments of HP0495. About 97% of all the $^1HN$, $^{15}N$, $^{13}C{\alpha}$, $^{13}C{\beta}$, and $^{13}CO$ resonances were assigned unambiguously. We could predict the secondary structure of HP0495, 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 HP0495 consists of two $\alpha$-helices and four $\beta$-strands. This study is a prerequisite for determining the solution structure of HP0495 and investigating the protein-protein interaction between HP0495 and other Helicobacter pylori proteins.

Protein Tertiary Structure Prediction Method based on Fragment Assembly

  • Lee, Julian;Kim, Seung-Yeon;Joo, Kee-Hyoung;Kim, Il-Soo;Lee, Joo-Young
    • 한국생물정보학회:학술대회논문집
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    • 한국생물정보시스템생물학회 2004년도 The 3rd Annual Conference for The Korean Society for Bioinformatics Association of Asian Societies for Bioinformatics 2004 Symposium
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    • pp.250-261
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    • 2004
  • A novel method for ab initio prediction of protein tertiary structures, PROFESY (PROFile Enumerating SYstem), is introduced. This method utilizes secondary structure prediction information and fragment assembly. The secondary structure prediction of proteins is performed with the PREDICT method which uses PSI-BLAST to generate profiles and a distance measure in the pattern space. In order to predict the tertiary structure of a protein sequence, we assemble fragments in the fragment library constructed as a byproduct of PREDICT. The tertiary structure is obtained by minimizing the potential energy using the conformational space annealing method which enables one to sample diverse low lying minima of the energy function. We apply PROFESY for prediction of some proteins with known structures, which shows good performances. We also participated in CASP5 and applied PROFESY to new fold targets for blind predictions. The results were quite promising, despite the fact that PROFESY was in its early stage of development. In particular, the PROFESY result is the best for the hardest target T0161.

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NDRG3-mediated lactate signaling in hypoxia

  • Park, Kyung Chan;Lee, Dong Chul;Yeom, Young Il
    • BMB Reports
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    • 제48권6호
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    • pp.301-302
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    • 2015
  • Hypoxia is associated with many pathological conditions as well as the normal physiology of metazoans. We identified a lactate-dependent signaling pathway in hypoxia, mediated by the oxygen- and lactate-regulated protein NDRG family member 3 (NDRG3). Oxygen negatively regulates NDRG3 expression at the protein level via the PHD2/VHL system, whereas lactate, produced in excess under prolonged hypoxia, blocks its proteasomal degradation by binding to NDRG3. We also found that the stabilized NDRG3 protein promotes angiogenesis and cell growth under hypoxia by activating the Raf-ERK pathway. Inhibiting cellular lactate production abolishes NDRG3-mediated hypoxia responses. The NDRG3-Raf-ERK axis therefore provides the genetic basis for lactate-induced hypoxia signaling, which can be exploited for the development of therapies targeting hypoxia-induced diseases in addition to advancing our understanding of the normal physiology of hypoxia responses. [BMB Reports 2015; 48(6): 301-302]