http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
- 中文 을 입력하시려면 zhongwen을 입력하시고 space를누르시면됩니다.
- 北京 을 입력하시려면 beijing을 입력하시고 space를 누르시면 됩니다.
RISS 인기검색어
- 검색키워드
- 저자 : Pannuru Venkatesu (검색결과 2 건)
- 무료
- 기관 내 무료
- 유료
-
Effects of Atmospheric-pressure Non-thermal Plasma Jets on Enzyme Solutions
Pankaj Attri,Pannuru Venkatesu,Kaushik NAgendra Kumar,Yong Gyu Han,Chul Joo Nam,최은하,김기선 한국물리학회 2012 THE JOURNAL OF THE KOREAN PHYSICAL SOCIETY Vol.60 No.6
In order to study the wide scope of structural information of biomolecules in the presence of biocompatible cold atmospheric pressure plasma jets (CAPJ), we used circular dichroism (CD) and fluorescence experiments. Biomolecules are very sensitive and are highly complex systems, exhibiting a substantial degree of structural variability in their folded state. In the present investigation, we compared the compatiblity of -chymotrypsin (CT) in the presence of biocompatible CAPJ. Using circular dichroism (CD) and fluorescence experiments, we describe the associated structural changes in CT after a 5 min treatment with CAPJ. The modifications in the secondary structure of this β/β protein were quantified by using the CD spectra. A reasonable decrease was observed for β-strands after treatment with CAPJ as compared to buffer, which contributes to its deterioration power. The implications of our results from studies delineating the effects of CAPJ on enzyme solutions are discussed.
-
Jha, Indrani,Attri, Pankaj,Venkatesu, Pannuru The Royal Society of Chemistry 2014 Physical chemistry chemical physics Vol.16 No.12
<P>The nature of solvent–biomolecule interactions is generally weak and non-specific. The addition of ionic liquids (ILs), which have emerged as a new class of solvents, strengthen the stability of some proteins whereas the same ILs weaken the stability of some other proteins. Although ILs are commonly used for the stabilization of biomolecules, the bimolecular interactions of their stabilization–destabilization is still an active subject of considerable interest and studies on this topic have been limited. To reveal the impact of ILs on the stability of proteins, a series of protic ILs possessing a tetra-alkyl ammonium cation [R<SUB>4</SUB>N]<SUP>+</SUP> with a hydroxide [OH]<SUP>−</SUP> anion were synthesized. In this study, we report the structural stability of heme proteins such as myoglobin (Mb) and hemoglobin (Hb) in a series of ammonium-based ILs such as tetramethyl ammonium hydroxide [(CH<SUB>3</SUB>)<SUB>4</SUB>N]<SUP>+</SUP>[OH]<SUP>−</SUP> (TMAH), tetraethyl ammonium hydroxide [(C<SUB>2</SUB>H<SUB>5</SUB>)<SUB>4</SUB>N]<SUP>+</SUP>[OH]<SUP>−</SUP> (TEAH), tetrapropyl ammonium hydroxide [(C<SUB>3</SUB>H<SUB>7</SUB>)<SUB>4</SUB>N]<SUP>+</SUP>[OH]<SUP>−</SUP> (TPAH) and tetrabutyl ammonium hydroxide [(C<SUB>4</SUB>H<SUB>9</SUB>)<SUB>4</SUB>N]<SUP>+</SUP>[OH]<SUP>−</SUP> (TBAH) by fluorescence and circular dichroism (CD) spectroscopic studies. Our experimental results reveal that less viscous ILs carrying smaller alkyl chain such as TMAH are strong destabilizers of the heme proteins as compared to the ILs carrying bulkier alkyl chains which are more viscous ILs, such as TBAH. Therefore, our results demonstrate that the addition of these ILs to the heme proteins decreases their thermal stability allowing the protein to be in an unfolded state at lower temperatures. Further, we describe the molecular–structural interaction of the heme proteins with the ILs (molecule like a ligand) by the PatchDocking method.</P> <P>Graphic Abstract</P><P>Ammonium-based ILs are shown to have a denaturing and destabilizing effect on heme proteins. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c3cp54398f'> </P>
연관 검색어 추천
이 검색어로 많이 본 자료
활용도 높은 자료
