• 제목/요약/키워드: protein structure analysis

검색결과 535건 처리시간 0.031초

An Approach for a Substitution Matrix Based on Protein Blocks and Physicochemical Properties of Amino Acids through PCA

  • You, Youngki;Jang, Inhwan;Lee, Kyungro;Kim, Heonjoo;Lee, Kwanhee
    • Interdisciplinary Bio Central
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    • 제6권4호
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    • pp.3.1-3.10
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    • 2014
  • Amino acid substitution matrices are essential tools for protein sequence analysis, homology sequence search in protein databases and multiple sequence alignment. The PAM matrix was the first widely used amino acid substitution matrix. The BLOSUM series then succeeded the PAM matrix. Most substitution matrixes were developed by using the statistical frequency of substitution between each amino acid at blocks representing groups of protein families or related proteins. However, substitution of amino acids is based on the similarity of physiochemical properties of each amino acid. In this study, a new approach was used to obtain major physiochemical properties in multiple sequence alignment. Frequency of amino acid substitution in multiple sequence alignment database and selected attributes of amino acids in physiochemical properties database were merged. This merged data showed the major physiochemical properties through principle components analysis. Using factor analysis, these four principle components were interpreted as flexibility of electronic movement, polarity, negative charge and structural flexibility. Applying these four components, BAPS was constructed and validated for accuracy. When comparing receiver operated characteristic ($ROC_{50}$) values, BAPS scored slightly lower than BLOSUM and PAM. However, when evaluating for accuracy by comparing results from multiple sequence alignment with the structural alignment results of two test data sets with known three-dimensional structure in the homologous structure alignment database, the result of the test for BAPS was comparatively equivalent or better than results for prior matrices including PAM, Gonnet, Identity and Genetic code matrix.

Protein-protein Interaction Analysis of Bradykinin Receptor B2 with Bradykinin and Kallidin

  • Nagarajan, Santhosh Kumar;Madhavan, Thirumurthy
    • 통합자연과학논문집
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    • 제10권2호
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    • pp.74-77
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    • 2017
  • Bradykinin receptor B2 (B2R) is a GPCR protein which binds with the inflammatory mediator hormone bradkynin. Kallidin, a decapeptide, also signals through this receptor. B2R is crucial in the cross-talk between renin-angiotensin system (RAS) and the kinin-kallikrein system (KKS) and in many processes including vasodilation, edema, smooth muscle spasm and pain fiber stimulation. Thus the structural study of the receptor becomes important. We have predicted the peptide structures of Bradykinin and Kallidin from their amino acid sequences and the structures were docked with the receptor structure. The results obtained from protein-protein docking could be helpful in studying the B2R structural features and in the pathophysiology in various diseases related to it.

MOTIF BASED PROTEIN FUNCTION ANALYSIS USING DATA MINING

  • Lee, Bum-Ju;Lee, Heon-Gyu;Ryu, Keun-Ho
    • 대한원격탐사학회:학술대회논문집
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    • 대한원격탐사학회 2006년도 Proceedings of ISRS 2006 PORSEC Volume II
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    • pp.812-815
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    • 2006
  • Proteins are essential agents for controlling, effecting and modulating cellular functions, and proteins with similar sequences have diverged from a common ancestral gene, and have similar structures and functions. Function prediction of unknown proteins remains one of the most challenging problems in bioinformatics. Recently, various computational approaches have been developed for identification of short sequences that are conserved within a family of closely related protein sequence. Protein function is often correlated with highly conserved motifs. Motif is the smallest unit of protein structure and function, and intends to make core part among protein structural and functional components. Therefore, prediction methods using data mining or machine learning have been developed. In this paper, we describe an approach for protein function prediction of motif-based models using data mining. Our work consists of three phrases. We make training and test data set and construct classifier using a training set. Also, through experiments, we evaluate our classifier with other classifiers in point of the accuracy of resulting classification.

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The Catalytic Subunit of Protein Kinase A Interacts with Testis-Brain RNA-Binding Protein (TB-RBP)

  • ;길성호
    • 대한의생명과학회지
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    • 제13권4호
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    • pp.305-311
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    • 2007
  • cAMP-dependent protein kinase A (PKA) is the best-characterized protein kinases and has served as a model of the structure and regulation of cAMP-binding protein as well as of protein kinases. To determine the function of PKA in development, we employed the yeast two-hybrid system to screen for catalytic subunit of PKA $(C\alpha)$ interacting partners in a cDNA library from mouse embryo. A Testis-brain RNA-binding protein (TB-RBP), specifically bound to $C\alpha$. This interaction was verified by several biochemical analysis. Our findings indicate that $C\alpha$ can modulate nucleic acid binding proteins of TB-RBP and provide insights into the diverse role of PKA.

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Characterization of Lipid Binding Region of Lipoprotein Lipase

  • Lee, Jae-Bok;Kim, Tae-Woong
    • Preventive Nutrition and Food Science
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    • 제4권2호
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    • pp.139-144
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    • 1999
  • Lipoprotein lipase (LPL) I san enzyme that catalyzed the hydrolysis of triacylglycerols of chylomicrons and VLDL to produce 20acylglycerols and fatty acids. The enzyme, LPL, is localized on the surface of the capillary endothelium and is widely distributed in extrahepatic tissues including heart, skeletal muscle and adipose tissue. LPL has been isolated from boving milk by affinity chromatography on heparin-separose in 2 M NaCL, 5mM barbital buffer, pH 7.4. To elucidate the lipid-binding regin, LPL was digested with trypsin and then separated by gel filtration. Lipid binding region of LPL has been investigated by recombining LPL peptides with DMPC vesicles. Proteolytic LPL fragments with DMPC were reassembled and stabilized by cholate. Lipid-binding region of LPL was identified by a PTH-automated protein sequencer, as AQQHYPVSAGYTK. The analysis of the secondary structure of the lipid-binding peptides revealed a higher probability of $\alpha$-helix structure compared to the whole LPL protein. The prediction of hydrophobicity of lipid -binding region was highly hydrophobic (-1.1) compared to LPL polypetide(-0.4).

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Helicobacter Pylori CagA and Gastric Carcinogenesis

  • Zheng, Ri-Nan;Li, Shu-Rong;Masahiro, Asaka
    • Asian Pacific Journal of Cancer Prevention
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    • 제13권12호
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    • pp.6305-6310
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    • 2012
  • Objectives: This study aimed to demonstrate the tyrosine phosphorylation motif (TPM) and 3' region structure of the Helicobacter pylori CagA gene as well as its SHP-2 binding activity in AGS cells and relation to gastric carcinogenesis. Methods: Sixteen clinical isolate H. pylori strains from eight duodenal ulcer and eight gastric adenocarcinoma patients were studied for CagA repeat sequence EPIYA motifs, C-terminal structure, and western blot analysis of CagA protein expression, translocation, and SHP-2 binding in AGS cells. Results: Except for strain 547, all strains from the gastric adenocarcinoma patients were positive for CagA by PCR and had three EPIYA copy motifs. Western blotting showed that all strains were positive for CagA protein expression (100%), CagA protein translocation (100%), and SHP-2 binding (100%). CagA protein expression was significantly higher in the gastric adenocarcinoma patients than in the duodenal ulcer patients (P=0.0023). CagA protein translocation and SHP-2 binding in the gastric adenocarcinoma patients were higher than those in the duodenal ulcer patients, but no significant differences were found between the two groups (P=0.59, P=0.21, respectively). Conclusions: The TPMs and 3' region structures of the H. pylori CagA gene in the duodenal ulcer and gastric adenocarcinoma patients have no significant differences.

Biochemical and Structural Analysis of Hormone-sensitive Lipase Homolog EstE7: Insight into the Stabilized Dimerization of HSL-Homolog Proteins

  • Nam, Ki-Hyun;Park, Sung-Ha;Lee, Won-Ho;Hwang, Kwang-Yeon
    • Bulletin of the Korean Chemical Society
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    • 제31권9호
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    • pp.2627-2632
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    • 2010
  • Hormone sensitive lipase (HSL) plays a major role in energy homeostasis and lipid metabolism. Several crystal structures of HSL-homolog proteins have been identified, which has led to a better understanding of its molecular function. HSL-homolog proteins exit as both monomer and dimer, but the biochemical and structural basis for such oligomeric states has not been successfully elucidated. Therefore, we determined the crystal structure of HSL-homolog protein EstE7 from a metagenome library at $2.2\;{\AA}$ resolution and characterized the oligomeric states of EstE7 both structurally and biochemically. EstE7 protein prefers the dimeric state in solution, which is supported by its higher enzymatic activity in the dimeric state. In the crystal form, EstE7 protein shows two-types of dimeric interface. Specifically, dimerization via the external ${beta}8$-strand occurred through tight association between two pseudosymmetric folds via salt bridges, hydrogen bonds and van der Waals interactions. This dimer formation was similar to that of other HSL-homolog protein structures such as AFEST, BEFA, and EstE1. We anticipate that our results will provide insight into the oligomeric state of HSL-homolog proteins.

Stability and Structure of S128A Mutant cAMP Receptor Protein

  • Choi, Young;Gang, JongBack
    • 통합자연과학논문집
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    • 제4권3호
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    • pp.222-226
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    • 2011
  • Cyclic AMP receptor protein(CRP) is involved in the activation of many genes corresponding to catabolite enzymes in Escherichia coli. In this study, mutant CRP(S128A) was used to elucidate the effect of Ser 128 on the cAMP-induced structural change. Based on the protease digestion and thermal analysis, serine 128 in CRP affects the cAMP binding capability and then structural change of CRP protein. In addition, CD spectra in near UV region revealed that S128A CRP retained the sensitive conformation to thermal effect relative to that of wild-type CRP, in spite of identical Tm values in the absence of cAMP.

Quinetides: diverse posttranslational modified peptides of ribonuclease-like storage protein from Panax quinquefolius as markers for differentiating ginseng species

  • Zhao, Qiang;Bai, Yunpeng;Liu, Dan;Zhao, Nan;Gao, Huiyuan;Zhang, Xiaozhe
    • Journal of Ginseng Research
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    • 제44권5호
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    • pp.680-689
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    • 2020
  • Background: Peptides have diverse and important physiological roles in plants and are ideal markers for species identification. It is unclear whether there are specific peptides in Panax quinquefolius L. (PQ). The aims of this study were to identify Quinetides, a series of diverse posttranslational modified native peptides of the ribonuclease-like storage protein (ginseng major protein), from PQ to explore novel peptide markers and develop a new method to distinguish PQ from Panax ginseng. Methods: We used different fragmentation modes in the LTQ Orbitrap analysis to identify the enriched Quinetide targets of PQ, and we discovered Quinetide markers of PQ and P. ginseng using ultrahigh-performance liquid chromatography-quadrupole time-of-flight mass spectrometry analysis. These "peptide markers" were validated by simultaneously monitoring Rf and F11 as standard ginsenosides. Results: We discovered 100 Quinetides of PQ with various post-translational modifications (PTMs), including a series of glycopeptides, all of which originated from the protein ginseng major protein. We effectively distinguished PQ from P. ginseng using new "peptide markers." Four unique peptides (Quinetides TP6 and TP7 as markers of PQ and Quinetides TP8 and TP9 as markers of P. ginseng) and their associated glycosylation products were discovered in PQ and P. ginseng. Conclusion: We provide specific information on PQ peptides and propose the clinical application of peptide markers to distinguish PQ from P. ginseng.

The targeting peptides for tumor receptor imaging

  • Yim, Min Su;Ryu, Eun Kyoung
    • 대한방사성의약품학회지
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    • 제2권2호
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    • pp.63-68
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    • 2016
  • Peptides have been developed for in vivo imaging probes against to the specific biomarker in the biological process of living systems. Peptide based imaging probes have been applied to identify and detect their active sites using imaging modalities, such as PET, SPECT and MRI. Especially, tumor receptor imaging with the peptides has been widely used to specific tumor detection. This review discusses the targeting peptides that have been successfully characterized for tumor diagnosis by receptor imaging.