Pub Date : 2014-08-20DOI: 10.2142/biophys.54.S212_4
C. Tardin, D. Mizuno
{"title":"2P106 AFM Probing Opioid Signalosome on Neuroblastoma(03. Membrane proteins,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"C. Tardin, D. Mizuno","doi":"10.2142/biophys.54.S212_4","DOIUrl":"https://doi.org/10.2142/biophys.54.S212_4","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"24 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"125932255","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2014-08-20DOI: 10.2142/BIOPHYS.54.S129_1
R. Iino
{"title":"2SEA-01 Importance of membrane pumps and channels: an introduction(2SEA Which is important for biophysicists, pump or channel?,Symposium,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"R. Iino","doi":"10.2142/BIOPHYS.54.S129_1","DOIUrl":"https://doi.org/10.2142/BIOPHYS.54.S129_1","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"35 5 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"130221258","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2014-08-20DOI: 10.2142/biophys.54.S238_6
Harshita Sharma, Fumihito Ohtani, Parmila Kumari, Deepti Diwan, Miho Suzuki, N. Nemoto, T. Aita, K. Nishigaki
{"title":"2P264 Global clustering of whole organisms enabled by the GP method(21A. Genome biology:Genome analysis,Poster)","authors":"Harshita Sharma, Fumihito Ohtani, Parmila Kumari, Deepti Diwan, Miho Suzuki, N. Nemoto, T. Aita, K. Nishigaki","doi":"10.2142/biophys.54.S238_6","DOIUrl":"https://doi.org/10.2142/biophys.54.S238_6","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"8 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"127126641","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2014-08-20DOI: 10.2142/BIOPHYS.54.S218_5
Mizuki Matsuzaki, A. Narita
{"title":"2P143 Investigating conditions for structure analysis of binding states of formin/mDia1 to the actin filament by electron microscopy(10. Muscle,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"Mizuki Matsuzaki, A. Narita","doi":"10.2142/BIOPHYS.54.S218_5","DOIUrl":"https://doi.org/10.2142/BIOPHYS.54.S218_5","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"33 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"127608696","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2014-08-20DOI: 10.2142/biophys.54.S268_1
Masaru Yoshino, Hiroshi Takahashi, K. Morita, T. Takagi, H. Amii, T. Kanamori, M. Sonoyama
We have reported successful reconstitution of bacteriorhodopsin (bR) into novel partially fluorinated phosphatidylcholine (diF4H10-PC) vesicles, in that the reconstituted bR has native-like higher order structure and photocycle. The present study on structural stability of the reconstituted bR demonstrated that 2D crystals as well as trimeric structure of bR molecules are maintained and no light-induced denaturation is observed up to ~40 °C, which is much higher than the gel-to-liquid crystalline phase transition temperature (5 °C) of pure diF4H10-PC bilayer. The high stability of the reconstituted bR in diF4H10-PC is in stark contrast with bR in DMPC showing phase transition-induced disassembly of bR molecules and remarkable denaturation by visible light.
{"title":"3P115 High stability of two-dimensional crystal of reconstituted bacteriorhodopsin in partially fluorinated phosphatidylcholine(03. Membrane proteins,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"Masaru Yoshino, Hiroshi Takahashi, K. Morita, T. Takagi, H. Amii, T. Kanamori, M. Sonoyama","doi":"10.2142/biophys.54.S268_1","DOIUrl":"https://doi.org/10.2142/biophys.54.S268_1","url":null,"abstract":"We have reported successful reconstitution of bacteriorhodopsin (bR) into novel partially fluorinated phosphatidylcholine (diF4H10-PC) vesicles, in that the reconstituted bR has native-like higher order structure and photocycle. The present study on structural stability of the reconstituted bR demonstrated that 2D crystals as well as trimeric structure of bR molecules are maintained and no light-induced denaturation is observed up to ~40 °C, which is much higher than the gel-to-liquid crystalline phase transition temperature (5 °C) of pure diF4H10-PC bilayer. The high stability of the reconstituted bR in diF4H10-PC is in stark contrast with bR in DMPC showing phase transition-induced disassembly of bR molecules and remarkable denaturation by visible light.","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"101 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"117191857","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2014-08-20DOI: 10.2142/BIOPHYS.54.S296_6
T. Katakura, R. Isonaka, T. Kawakami
{"title":"3P288 A new quantitative method to evaluate the activity of axonal transport of cultured neurons(26. Measurements,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"T. Katakura, R. Isonaka, T. Kawakami","doi":"10.2142/BIOPHYS.54.S296_6","DOIUrl":"https://doi.org/10.2142/BIOPHYS.54.S296_6","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"64 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"122629119","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2014-08-20DOI: 10.2142/BIOPHYS.54.S116_3
Satoshi Takahashi
{"title":"1SBA-02 Continuous tracking of protein folding at microsecond resolution by a line confocal detection of single molecule fluorescence(1SBA Regulating structure formation and function of biomolecular systems with softness,Symposium,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"Satoshi Takahashi","doi":"10.2142/BIOPHYS.54.S116_3","DOIUrl":"https://doi.org/10.2142/BIOPHYS.54.S116_3","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"78 6","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"132463155","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2014-08-20DOI: 10.2142/BIOPHYS.54.S257_4
Y. Maruyama, A. Mitsutake
{"title":"3P052 Analysis for the structural stability of chignolin(01C. Protein: Property,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"Y. Maruyama, A. Mitsutake","doi":"10.2142/BIOPHYS.54.S257_4","DOIUrl":"https://doi.org/10.2142/BIOPHYS.54.S257_4","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"41 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"126786186","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2014-08-20DOI: 10.2142/BIOPHYS.54.S259_1
K. Sakurai, M. Yagi, C. Nishimura, K. Akasaka, Y. Goto
Bovine β-lactoglobulin (βLG) has a folding intermediate with a non-native α-helical structure. Our previous study indicated that the moderate αhelical propensity of the wild-type sequence likely contributes to circumventing non-productive intermediates. In the present study, we analyzed the dynamics of the denatured βLG and performed high-pressure NMR measurements and H/D exchange pulse labeling experiments to obtain structural information of the intermediates. The results suggested that the three portions of the sequence, the C-terminal, the middle, and the N-terminal regions, sequentially attain individual native structures. Probably, the order of folding of these regions is programed in the βLG sequence to avoid non-native aggregations.
{"title":"3P061 The circumventing mechanism of the folding of β-lactoglobulin(01C. Protein: Property,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"K. Sakurai, M. Yagi, C. Nishimura, K. Akasaka, Y. Goto","doi":"10.2142/BIOPHYS.54.S259_1","DOIUrl":"https://doi.org/10.2142/BIOPHYS.54.S259_1","url":null,"abstract":"Bovine β-lactoglobulin (βLG) has a folding intermediate with a non-native α-helical structure. Our previous study indicated that the moderate αhelical propensity of the wild-type sequence likely contributes to circumventing non-productive intermediates. In the present study, we analyzed the dynamics of the denatured βLG and performed high-pressure NMR measurements and H/D exchange pulse labeling experiments to obtain structural information of the intermediates. The results suggested that the three portions of the sequence, the C-terminal, the middle, and the N-terminal regions, sequentially attain individual native structures. Probably, the order of folding of these regions is programed in the βLG sequence to avoid non-native aggregations.","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"180 2","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2014-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"114004743","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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