Pub Date : 2014-08-20DOI: 10.2142/BIOPHYS.54.S257_1
A. Hirano, T. Arakawa, T. Kameda
Arginine is effective in elution of proteins from chromatography columns. In this study, effects of arginine on the elution from multimodal chromatography columns, the resins of which have multiple functional groups, were examined using bovine serum albumin and a monoclonal antibody against interleukin-8. The resins used here were Capto MMC and Capto adhere, which are multimodal cation and anion exchangers, respectively. As expected, arginine effectively eluted the proteins from the columns. Mechanism of the elution was examined by molecular dynamics simulations. The results showed that the affinity of arginine was primarily associated with electrostatic interaction for Capto MMC and with hydrophobic and π-π interactions as well as hydrogen bonding for Capto adhere.
{"title":"3P049 Multimodal chromatography of proteins in arginine solutions(01C. Protein: Property,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"A. Hirano, T. Arakawa, T. Kameda","doi":"10.2142/BIOPHYS.54.S257_1","DOIUrl":"https://doi.org/10.2142/BIOPHYS.54.S257_1","url":null,"abstract":"Arginine is effective in elution of proteins from chromatography columns. In this study, effects of arginine on the elution from multimodal chromatography columns, the resins of which have multiple functional groups, were examined using bovine serum albumin and a monoclonal antibody against interleukin-8. The resins used here were Capto MMC and Capto adhere, which are multimodal cation and anion exchangers, respectively. As expected, arginine effectively eluted the proteins from the columns. Mechanism of the elution was examined by molecular dynamics simulations. The results showed that the affinity of arginine was primarily associated with electrostatic interaction for Capto MMC and with hydrophobic and π-π interactions as well as hydrogen bonding for Capto adhere.","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"18 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":"131981925","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.S250_1
R. Tanaka, K. Yoshizawa, Tomonobu M. Watanabe, T. Kawaguchi, K. Imada
YFP is a mutant derivative of green fluorescent protein, and is widely used as a fluorescent indicator in molecular biology. Recently we found that YFP mutant variants with single amino acid insertion in β7 showed various fluorescence responses to environmental change. The fluorescence responses depend on the nature of the inserted amino acid residue. To elucidate the molecular mechanism how the insertion affects the fluorescent property, we prepared twenty single amino acid insertion variants of YFP and solved the structures. Here we show the structures of eighteen mutant YFPs. They show unexpected conformational variation in β7 dependent on the inserted residue. We will discuss the relationship between the mutant structure and the fluorescent property.
{"title":"3P007 Systematic structural study of single amino acid insertion mutants of YFP(01A. Protein: Structure,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"R. Tanaka, K. Yoshizawa, Tomonobu M. Watanabe, T. Kawaguchi, K. Imada","doi":"10.2142/BIOPHYS.54.S250_1","DOIUrl":"https://doi.org/10.2142/BIOPHYS.54.S250_1","url":null,"abstract":"YFP is a mutant derivative of green fluorescent protein, and is widely used as a fluorescent indicator in molecular biology. Recently we found that YFP mutant variants with single amino acid insertion in β7 showed various fluorescence responses to environmental change. The fluorescence responses depend on the nature of the inserted amino acid residue. To elucidate the molecular mechanism how the insertion affects the fluorescent property, we prepared twenty single amino acid insertion variants of YFP and solved the structures. Here we show the structures of eighteen mutant YFPs. They show unexpected conformational variation in β7 dependent on the inserted residue. We will discuss the relationship between the mutant structure and the fluorescent property.","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"118 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":"134174626","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.S216_3
Yukinobu Mizuhara, K. Umezawa, J. Ohnuki, D. Parkin, M. Takano
{"title":"2P129 Critical parameters of the generalized Born model to simulate protein-protein interactions(07. Water & Hydration & Electrolyte,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"Yukinobu Mizuhara, K. Umezawa, J. Ohnuki, D. Parkin, M. Takano","doi":"10.2142/BIOPHYS.54.S216_3","DOIUrl":"https://doi.org/10.2142/BIOPHYS.54.S216_3","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"11 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":"131019784","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.S148_2
Mai Tsunoda, Muneyo Mio, T. Sugiki, K. Mio
{"title":"1P044 Molecular basis of conformational dynamics and enzymatical maturation process of nuclear lamin A related to onset of laminopathies(01B. Protein : Structure & Function,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"Mai Tsunoda, Muneyo Mio, T. Sugiki, K. Mio","doi":"10.2142/biophys.54.S148_2","DOIUrl":"https://doi.org/10.2142/biophys.54.S148_2","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"54 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":"130990758","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.S165_6
H. Ueno, B. Khanh, T. Ishikawa
{"title":"1P150 Structure of dimeric axonemal dynein in cilia suggests an alternative mechanism of force generation(11. Molecular motor,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"H. Ueno, B. Khanh, T. Ishikawa","doi":"10.2142/BIOPHYS.54.S165_6","DOIUrl":"https://doi.org/10.2142/BIOPHYS.54.S165_6","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"123 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":"132829235","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.S300_3
A. Jasaitis, G. Clouvel, I. Izeddin, J. Sillibourne, M. El-Beheiry, X. Levecq, M. Dahan, M. Bornens, X. Darzacq
{"title":"3P309 3D Palm Imaging at 50 Micrometers Depth in the Sample(27. Bioimaging,Poster,The 52nd Annual Meeting of the Biophysical Society","authors":"A. Jasaitis, G. Clouvel, I. Izeddin, J. Sillibourne, M. El-Beheiry, X. Levecq, M. Dahan, M. Bornens, X. Darzacq","doi":"10.2142/BIOPHYS.54.S300_3","DOIUrl":"https://doi.org/10.2142/BIOPHYS.54.S300_3","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"13 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":"133023201","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.S273_1
N. Isozaki, S. Ando, H. Shintaku, H. Kotera, E. Meyhofer, R. Yokokawa
A challenge for using microtubules (MTs) driven by kinesin motors in functional nanosystems is to control their direction of movement. A method was developed to guide kinesin-propelled MTs in multiple directions under an electric field by designing a charged surface of MT minus ends labeled with dsDNA via a streptavidin-biotin interaction. Experimental trajectories were in good agreement with values predicted from measured electrophoretic mobilities. As the effective charge of labeled DNA molecules matches to that of freely dispersed DNA molecules, MT trajectory can be estimated even by selecting labeling molecules with known charges. Our molecular design and prediction methodology demonstrate the feasibility of using molecular sorters driven by motor proteins.
{"title":"3P145 Control of microtubule trajectory within an electric field by altering surface charge density(11. Molecular motor,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"N. Isozaki, S. Ando, H. Shintaku, H. Kotera, E. Meyhofer, R. Yokokawa","doi":"10.2142/BIOPHYS.54.S273_1","DOIUrl":"https://doi.org/10.2142/BIOPHYS.54.S273_1","url":null,"abstract":"A challenge for using microtubules (MTs) driven by kinesin motors in functional nanosystems is to control their direction of movement. A method was developed to guide kinesin-propelled MTs in multiple directions under an electric field by designing a charged surface of MT minus ends labeled with dsDNA via a streptavidin-biotin interaction. Experimental trajectories were in good agreement with values predicted from measured electrophoretic mobilities. As the effective charge of labeled DNA molecules matches to that of freely dispersed DNA molecules, MT trajectory can be estimated even by selecting labeling molecules with known charges. Our molecular design and prediction methodology demonstrate the feasibility of using molecular sorters driven by motor proteins.","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"198 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":"133688650","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.S156_5
T. Matsui, S. Nambu, M. Ikeda-Saito
{"title":"1P095 Unique reaction mechanism of MhuD, a heme-degrading enzyme from Mycobacterial tuberculosis(02. Heme proteins,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"T. Matsui, S. Nambu, M. Ikeda-Saito","doi":"10.2142/biophys.54.S156_5","DOIUrl":"https://doi.org/10.2142/biophys.54.S156_5","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"76 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":"133455941","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.S300_4
Y. Takayama, S. Maki-Yonekura, Tomotaka Oroguchi, M. Nakasako, K. Yonekura
{"title":"3P310 Signal enhancement and Patterson-search phasing for highspatial-resolution coherent X-ray diffraction imaging of biological objects(27. Bioimaging,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"Y. Takayama, S. Maki-Yonekura, Tomotaka Oroguchi, M. Nakasako, K. Yonekura","doi":"10.2142/biophys.54.S300_4","DOIUrl":"https://doi.org/10.2142/biophys.54.S300_4","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"10 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":"132764752","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.S206_5
C. Lim, Y. Furukawa
{"title":"2P071 An activation mechanism of human Cu,Zn-superoxide dismutase by its copper chaperone, CCS(01D. Protein: Function,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))","authors":"C. Lim, Y. Furukawa","doi":"10.2142/BIOPHYS.54.S206_5","DOIUrl":"https://doi.org/10.2142/BIOPHYS.54.S206_5","url":null,"abstract":"","PeriodicalId":409321,"journal":{"name":"Seibutsu Butsuri","volume":"26 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":"133119545","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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