• 한국정보통신학회논문지
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• 제19권12호
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• pp.3011-3016
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• 2015

단백질의 삼차원 구조를 단백질의 국부적 구조인 단백질 조각의 일차원적 나열로 표현하면, 단백질 구조의 분석, 모델링, 탐색, 예측 등에 효과적으로 응용될 수 있다. 본 논문에서는 자연 상태의 단백질 구조를 정확하게 나타낼 수 있는 단백질 조각 라이브러리를 구성하기 위하여, 대규모 단백질 구조 자료를 이용 할 수 있는 거리 척도들의 효과적인 조합을 조사하였다. 단백질 조각 라이브러리를 구성하기 위해 군집화를 사용하였다. 초기 군집화 단계에서는 가장 계산량이 작은 내부 알파탄소간 거리를 사용하였고, 군집의 확장단계에서는 내부 알파탄소간 거리, 비네-코시거리와 평균 제곱근 오차를 조합하여 사용하였다. 제안한 거리 척도의 조합으로 대규모 자료를 이용하여 단백질 조각 라이브러리를 구성하였다. 구성된 라이브러리를 사용하여 단백질 구조를 나타내는 실험에서 작은 평균 제곱근 오차가 발생함을 확인하였다.

• BMB Reports
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• 제42권11호
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• pp.697-704
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• 2009

Membrane proteins play important roles in the biology of the cell, including intercellular communication and molecular transport. Their well-established importance notwithstanding, the high-resolution structures of membrane proteins remain elusive due to difficulties in protein expression, purification and crystallization. Thus, accurate prediction of membrane protein topology can increase the understanding of membrane protein function. Here, we provide a brief review of the diverse computational methods for predicting membrane protein structure and function, including recent progress and essential bioinformatics tools. Our hope is that this review will be instructive to users studying membrane protein biology in their choice of appropriate bioinformatics methods.

• 한국자기공명학회논문지
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• 제15권1호
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• pp.80-89
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• 2011

3D structures of STAM1 UIM-ubiquitin complex were presented to predict and analyze the interaction between UIM and ubiquitin. To generate the protein-peptide complex structure, the RosettaDock method was used with and without NMR restraints. High resolution complex structure was acquired successfully and evaluated electrostatic interaction in the protein-peptide binding with several charged residues at the binding site. From docking results, the Rosettadock method could be useful to acquire essential information of protein-protein or protein-peptide interaction with minimal biological evidences.

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 1996년도 정기총회 및 학술발표회
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• pp.11-11
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• 1996

The three-dimensional structure of the carboxyl-terminal domain of the E.coli RNA polymerase $\alpha$ subunit, which is regarded as the contact site for transcription activator proteins and the promoter UP element, was determined by NMR spectroscopy. Its compact structure of four helices and two long arms enclosing its hydrophobic core shows a folding topology distinct from those of other DNA-binding proteins. (omitted)

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 2003년도 정기총회 및 학술발표회
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• pp.65-65
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• 2003

After many genome projects, algorithms and software to process explosively growing biological information have been developed. To process huge amount of biological information, high performance computing equipments are essential. If we use the remote resources such as computing power, storages etc., through a Grid to share the resources in the Internet environment, we will be able to obtain great efficiency to process data at a low cost. Here we present the performance improvement of the protein secondary structure prediction (PSIPred) by using the Grid platform, distributing protein sequence data on the Grid where each computer node analyzes its own part of protein sequence data to speed up the structure prediction. On the Grid, genome scale secondary structure prediction for Mycoplasma genitalium, Escherichia coli, Helicobacter pylori, Saccharomyces cerevisiae and Caenorhabditis slogans were performed and analyzed by a statistical way to show the protein structural deviation and comparison between the genomes. Experimental results show that the Grid is a viable platform to speed up the protein structure prediction and from the predicted structures.

• 컴퓨터교육학회논문지
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• 제12권4호
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• pp.57-64
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• 2009

단백질 구조 비교는 각 단백질에 존재하는 수많은 원자들을 처리해야 하므로 많은 컴퓨팅 자원을 요구하는 작업이다. 이러한 작업을 처리하기 위한 접근법으로써 그리드 환경에서 시간 소모가 큰 계산 작업을 분산 처리하는 것이 널리 사용되어 왔다. 그러나 이러한 그리드 환경을 통제하는 것은 비전문가들에게 쉽지 않을 수 있다. 본 논문에서는 비전문가들도 쉽게 그리드 환경을 통제할 수 있는 JXTA 기반의 단백질 구조 비교 시스템을 제안한다. 쿼리 단백질과 비슷한 단백질들을 찾기 위해 사전처리 단계 와 인식단계로 구성된 기하학적 해싱 알고리즘이 사용되었다. 실험 결과에 의하면 주어진 쿼리 단백질 구조와 일치하는 단백질 구조를 시스템이 정확히 찾고 또한 제안된 시스템은 쉽게 단백질 다킹 문제를 해결하도록 확장될 수도 있다. 본 논문에서 제안하는 시스템은 비전문가들, 특히 생물학이나 화학을 전공하는 대학생들처럼 일반적으로 분산 시스템에 대한 숙련된 지식이 없는 사용자들에게 도움이 되리라 기대된다.

• Bulletin of the Korean Chemical Society
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• 제32권5호
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• pp.1640-1644
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• 2011

Water-soluble mutant of intrinsically insoluble protein, crambin, was produced by mutagenesis based on the sequence analysis with homologous proteins. Thr1, Phe13, and Lys33 of crambin were substituted for Lys, Tyr, and Lys, respectively. The resultant mutant was soluble in aqueous buffer as well as in dodecylphosphocholine (DPC) micelle solution. The $^1H-^{15}N$ spectrum of the mutant crambin showed spectral similarity to that of the wild-type protein except for local regions proximal to the sites of mutation. Solution structure of water-soluble mutant crambin was determined in aqueous buffer by NMR spectroscopy. The structure was almost identical to the wild-type structure determined in non-aqueous solvent. Subtle difference in structure was very local and related to the change of the intra- and inter-protein hydrophobic interaction of crambin. The structural details for the enhanced solubility of crambin in aqueous solvent by the mutation were provided and discussed.

• 정보처리학회논문지:소프트웨어 및 데이터공학
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• 제3권4호
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• pp.163-168
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• 2014

단백질 분자 내에서 ${\alpha}$-헬릭스는 단백질의 구조나 기능, 그리고 다른 단백질과의 결합, 활성 조절 등에 있어 중요한 역할을 하며, 이에 따라 헬릭스에 대한 구조적인 분석이 연구되어 왔다. ${\alpha}$-헬릭스는 그 중심축을 기준으로 다른 ${\alpha}$-헬릭스와의 상호위치를 평가하기 때문에 길게 휘어지거나 꺾인 ${\alpha}$-헬릭스들을 한 개의 헬릭스로 해석할 경우에는 단백질의 구조 분석에 있어서 상당한 오차가 발생할 수 있다. 본 논문에서는 PDB 파일 내에 표시된 단백질 분자의 ${\alpha}$-헬릭스를 주어진 오차 범위 내에서 여러 개의 곧은 형태의 헬릭스로 재구성하는 알고리즘을 제안한다.

• 한국자기공명학회논문지
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• 제19권3호
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• pp.149-155
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• 2015

Acyl carrier protein is related with fatty acid biosynthesis in which specific enzymes are involved. Especially, acyl carrier protein (ACP) is the key component in the growing of fatty acid chain. ACP is the small, very acidic protein that covalently binds various intermediates of fatty acyl chain. Acylation of ACP is mediated by holo-acyl carrier protein synthase (ACPS), which transfers the 4'PP-moiety of CoA to the 36th residue Ser of apo ACP. Acyl carrier protein P (ACPP) is one of ACPs from Helicobacter plyori. The NMR structure of ACPP consists of four helices, which were reported previously. Here we show how acylation of ACPP can affect the overall structure of ACPP and figured out the contact surface of ACPP to acyl chain attached during expression of ACPP in E. coli. Based on the chemical shift perturbation data, the acylation of ACCP seems to affect the conformation of the long loop connecting helix I and helix II as well as the second short loop connecting helix II and helix III. The significant chemical shift change of Ile 54 upon acylation supports the contact of acyl chain and the second loop.

• 한국자기공명학회논문지
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• 제18권1호
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• pp.36-40
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• 2014

Predicting secondary structure of protein through assigned backbone chemical shifts has been used widely because of its convenience and flexibility. In spite of its usefulness, chemical shift based analysis has some defects including isotopic shifts and solvent interaction. Here, it is shown that corrected chemical shift analysis for secondary structure of protein. It is included chemical shift correction through consideration of deuterium isotopic effect and calculate chemical shift index using probability-based methods. Enhanced method was applied successfully to one of the proteins from Mycobacterium tuberculosis. It is suggested that correction of chemical shift analysis could increase accuracy of secondary structure prediction of protein and small molecule in solution.