• 제목/요약/키워드: Structural protein

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Structural Studies on RUNX of Caenorhabditis elegans by Spectroscopic Methods

  • Son, Woo-Sung;Kim, Jong-Wan;Ahn, Hee-Chul;Park, Sung-Jean;Bae, Suk-Chul;Lee, Bong-Jin
    • 한국자기공명학회논문지
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    • 제6권1호
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    • pp.54-68
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    • 2002
  • PEBP2/CBF (Polyomavirus Enhancer-core Binding Protein 2/Core Binding Factor), represents a new family of heterodimeric transcription factor. Those members play important roles in hematopoiesis and osteogenesis in mouse and human. PEBP2/CBF is a sequence-specific DNA binding protein. Each member of the PEBP2/CBF family of transcription factors is composed of two subunits, ${\alpha}$ and ${\beta}$. The evolutionarily conserved 128 amino acid region in ${\alpha}$ subunit has been called the Runt domain, which harbors two different activities, the ability to bind DNA and interact with the ${\beta}$ subunit. Recently, cDNA clones encoding the C. elegans Runt domain were isolated by screening a cDNA library. This gene was referred to run (Runt homologous gene). In this study, the basic experiments for the structural characterization of RUN protein were performed using spectroscopic methods. We have identified the structural properties of RUN using bioinformatics, CD and NMR. The limit temperature of the structural stability was up to 60$^{\circ}C$ with irreversible thermal process, and the structure of RUN seems to adopt ${\alpha}$ helices and one or more ${\beta}$ sheet or turn. The degree of NMR peak dispersion and intensity was increased by addition of glycine. Therefore, glycine could be used to alleviate the aggregation property of RUN in NMR experiment.

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박테리오파지 f2에 대한 자외광선의 살균효과 (The Inactivation Effects of UV Light on Bacteriophage f2)

  • Kim, Chi-Kyung;Quae Chae
    • 한국미생물·생명공학회지
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    • 제11권3호
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    • pp.155-161
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    • 1983
  • Bacteriophage f2에 대한 자외광선의 살균효과와 외투막 단백질의 구조에 미치는 영향을 Ray-onet photoreactor PPR-208을 사용하여 300nm의 광선으로 연구하였다. 처음 20분간의 조사에서는 약 4 log의 phage가 감소되고 그후 완만한 살균효과를 보이다가 90분 이상의 조사에서는 생존 바이러스가 발견되지 않았다. Tryptophan residue의 fluorescenve quenching, 자외선으로 조신한 phage에 부착시킨 ANS (8-anilino-1-napht-halene sulfonate)의 fluorescence emission의 감소, tryptophan에서 ANS로의 energy transfer 의 감소 등 spectroscopic technique에 의한 결과와 자외선 조사에 의하여 단백질 외투만이 파손되는 전자현미경 관찰의 결과에 의하여 자외광선은 phage f2의 외투막 단백질의 구조에 변화를 일으킨다는 것이 밝혀졌다.

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플루란 아세테이트 미립구를 이용한 단백질 전달 시스템 개발 (Development of Protein Delivery System using Pullulan Acetate Microspheres (PAM))

  • 나건;최후균
    • Journal of Pharmaceutical Investigation
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    • 제36권2호
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    • pp.115-121
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    • 2006
  • The aim of this study was to develop new protein/peptide depot system instead of poly(DL-lactic acid-coglycolic acid) (PLGA) microspheres. Pullulan was chemically modified by the addition of acetic anhydride (pullulan acetate; PA) and then investigated as new depot system for protein/peptide delivery. PA microspheres (PAM) with lysozyme as a model protein were prepared by w/o/w double emulsion method. The microspheres had a mean size of 10-50 mm with a spherical shape. The size distributions reduced with increasing the degree of acetylation. The loading efficiency of lysozyme was also increased. Lysozyme aggregation behavior in the microsphere was monitored to estimate the change of protein stability during preparation step. The ratios of protein aggregation in PAMs are lower than that of PLGA microsphere, in particular, PA 5 showed lowest as about 16%. The result indicated that the increase of acetylation suppressed the aggregation of protein. The release profiles of lysozyme from PAMs were significantly different. High acetylation effectively improved lysozyme release kinetics by reducing initial burst release and extending continuous release over a period of time. To check the effect of preservation for structural stability of lysozyme, the activity of lysozyme released from PA 5 was also observed. The activity of lysozyme was maintained almost 100% for 25 day. Therefore, PAM may become to a useful carrier for delivery of protein/peptide drugs, if it will be supported by biocompatibility and biodegradability results.