{"id":162,"date":"2015-12-08T15:37:07","date_gmt":"2015-12-08T06:37:07","guid":{"rendered":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/?page_id=162"},"modified":"2015-12-08T15:42:29","modified_gmt":"2015-12-08T06:42:29","slug":"%e8%ab%96%e6%96%87%e7%b4%b9%e4%bb%8b2014","status":"publish","type":"page","link":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/seminar\/%e8%ab%96%e6%96%87%e7%b4%b9%e4%bb%8b2014\/","title":{"rendered":"\u8ad6\u6587\u7d39\u4ecb2014"},"content":{"rendered":"

\"\"\u00a0No.36\u30002015.3.16
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u4f0a\u85e4\u512a\u5fd7
\n\u8ad6\u6587<\/strong>\uff1a<\/b>Microsecond Folding and Domain Motions of a Spider Silk Protein Structural Switch
\nJulia Ries et al.
\nJ. Am. Chem. Soc. 2014, 136, 17136-17144<\/p>\n

\"\"\u00a0No.35\u30002015.3.9
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u6751\u7530\u5d07\u4eba
\n\u8ad6\u6587<\/strong>\uff1a<\/b>Dynamics of translation by single ribosomes through mRNA secondary structures
\nChunlai Chen et al.
\nNature structural & molecular biology<\/em><\/div>\n

 <\/p>\n

\"\"\u00a0No.34\u30002015.2.23
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u9f4a\u85e4\u96c5\u5d69
\n\u8ad6\u6587<\/strong>\uff1a<\/b>The assembly dynamics of the cytolytic pore toxin ClyA
\nStephan Benke et al.
\nNature Communications<\/em> (2015)<\/div>\n

 <\/p>\n

\"\"\u00a0No.33\u30002015.2.16
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u938c\u5f62\u6e05\u4eba
\n\u8ad6\u6587<\/strong>\uff1a<\/b>The heat released during catalytic turnover enhances the diffusion of an enzyme
\nClement Riedel et al.
\nNature 517, <\/i>227-230, 2015<\/p>\n

\"\"\u00a0No.32\u30002015.2.2
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u5c0f\u4e95\u5ddd\u6d69\u4e4b
\n\u8ad6\u6587<\/strong>\uff1a<\/b>Protein conformational dynamics dicate the binding affinity for a ligand
\nNoon-Hyeong Seo et al.
\nNature Communications 5, <\/i>Article number:3724,2014<\/p>\n

\"\"\u00a0No.31\u30002015.1.26
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u9ad8\u6a4b\u8061
\n\u8ad6\u6587<\/strong>\uff1a\u00a0<\/b>Modulation of folding energy landscape by charge-charge interactions: Linking experiments with computational modeling
\nFranco O. Tzul et al.
\nPNAS,<\/em>2015, E259-E266<\/p>\n

\"\"\u00a0No.30\u30002015.1.19
\n\u62c5\u5f53\u8005<\/strong>\uff1aSubekti Rendra Graha Dwiky
\n\u8ad6\u6587<\/strong>\uff1a <\/b>The Covalent Trimethoprim Chemical tag Facilitates Single Molecule Imaging with Organic Fluophores
\ntracy Y. Wang et al.
\nBiophysical Journal<\/em>, Volume 106, january 2014, 272-278<\/p>\n

\"\"\u00a0No.29\u30002015.1.5
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u5c0f\u91ce\u5bfa\u967d\u592a\u6717
\n\u8ad6\u6587<\/strong>\uff1aNonuniform chain collapse during early stages of staphylococcal nuclease folding detected by fluorescence resonance energy transfer and ultrarapid mixing methods.
\nMizukami T et al.
\nProtein Sci. <\/em>2013 Oct;22 (10):1336-48<\/p>\n

\"\"\u00a0No.28\u30002014.12.15
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u4e94\u5341\u5d50\u5343\u88d5
\n\u8ad6\u6587<\/strong>\uff1aInteraction of p53 with the CCT Complex Promotes Protein Folding and Wild-Ype p53 Activity
\nAntonio Garcia Trinidad et al.
\nMolecular Cell<\/em>,2013<\/p>\n

\"\"\u00a0No.27\u30002014.12.8
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u6751\u7530\u5d07\u4eba
\n\u8ad6\u6587<\/strong>\uff1aA viral packaging motor varies its DNA rotation and step size to preserve subunit coordination as the capsid fills
\nShixin Liu et al.
\nCell<\/em>, 2014<\/p>\n

\"\"\u00a0No.26\u30002014.11.17
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u9f4a\u85e4\u96c5\u5d69
\n\u8ad6\u6587<\/strong>\uff1aSingle-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein
\nRuth Kellner et al.
\nPNAS<\/em>,vol.111, no.37 (2014)<\/p>\n

\"\"\u00a0No.25\u30002014.11.10
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u938c\u5f62\u6e05\u4eba
\n\u8ad6\u6587<\/strong>\uff1aProtein painting reveals solvent-excluded drug targets hidden within native protein-protein interfaces
\nAlessandra Luchini et al.
\nNature Communications<\/em>, 5:4413, doi: 10.1038, ncomms5413 (2014)<\/p>\n

\"\"\u00a0No.24\u30002014.10.27
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u5c0f\u4e95\u5ddd\u6d69\u4e4b
\n\u8ad6\u6587<\/strong>\uff1aDari Field Microspectroscopy with Single Molecule Fluorescence Sensitivity
\nAlexander Weigel et al.
\nACS Photonics<\/em>, 2014,1(9),pp 848-856<\/p>\n

\"\"\u00a0No.23\u30002014.10.20
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u9ad8\u6a4b\u8061
\n\u8ad6\u6587<\/strong>\uff1aEnergetically significant networks of coupled interactions within an unfolded protein
\nJae-Hyun Cho et al.
\nPNAS<\/em>, 2014,vol.111, no.33, 12079-12084<\/p>\n

\"\"\u00a0No.22\u30002014.10.6
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u5409\u7530\u6587
\n\u8ad6\u6587<\/strong>\uff1aEvidence for close side-chain packing in an early protein folding intermediate previously assumed to be a molten globule
\nRosen, Laura E. et al.
\nProceedings of the National Academy of Sciences <\/em>(2014) 201410630<\/p>\n

\"\"\u00a0No.21\u30002014.9.22
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u6751\u7530\u5d07\u4eba
\n\u8ad6\u6587<\/strong>\uff1aMicron-scale coherence in interphase chromatin dynamics
\nAlexandra Zidovska et al.
\nPNAS<\/em>, 2013, Sep 24;110(39):15555-60<\/p>\n

\"\"\u00a0No.20\u30002014.9.8
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u9ad8\u6a4b\u5f8b\u4e45
\n\u8ad6\u6587<\/strong>\uff1aStructure and Flexibility of Nanoscale Protein Cages Designed by Symmetric Self-Assembly
\nYen-Ting Lai et al.
\nJACS<\/em>, 2013, 135, 7738-7743<\/p>\n

\"\"\u00a0No.19\u30002014.9.1
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u4e94\u5341\u5d50\u5343\u88d5
\n\u8ad6\u6587<\/strong>\uff1aHow environmental solution conditions determine the compaction velocity of single DNA molecules
\nken Hirano et al.
\nNucleic. Acids Research<\/em>, 2011, 1-6<\/p>\n

\"\"\u00a0No.18\u30002014.8.25
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u5c0f\u91ce\u5bfa\u967d\u592a\u6717
\n\u8ad6\u6587<\/strong>\uff1aSubdomain-Specific Collapse of Denatured Staphylococcal Nuclease Revealed by Single Molecule Fluorescence Resonance Energy Transfer Measurements
\nPengcheng Liu et al.
\nJ. Phys. Chem. B<\/em> (2009) 113,12030-12036<\/p>\n

\"\"\u00a0No.17\u30002014.8.18
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u5207\u53e3\u7406\u6075
\n\u8ad6\u6587<\/strong>\uff1aA New Protein-Protein Interaction Sensor Based on Tripartite Split-GFP Association
\nStephanie Cabantous et al.
\nScientific Reports <\/em>(2013)<\/p>\n

\"\"\u00a0No.16\u30002014.8.4
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u4f0a\u85e4\u512a\u5fd7
\n\u8ad6\u6587<\/strong>\uff1aRedefining the Dry Molten Globule State of Proteins
\nSabine Neumaier and Thomas Kiefhaber
\nJ. Mol. Biol.<\/em> (2014) 426,2520-2528<\/p>\n

\"\"\u00a0No.15\u30002014.7.28
\n\u62c5\u5f53\u8005<\/strong>\uff1aSubekti Rendra Graha Dwiky
\n\u8ad6\u6587<\/strong>\uff1aProtein activity regulation by conformational entropy
\nShiou0Ru Tzeng & Charalampos G. kalodimos
\nNature<\/em>, Vol.488, 236-240 (2012)<\/p>\n

\"\"\u00a0No.14\u30002014.7.14
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u9f4a\u85e4\u96c5\u5d69
\n\u8ad6\u6587<\/strong>\uff1aVisualizing transient protein-folding intermediates by tryptophan-scanning mutagenesis
\nNature Structural & Molecular Biology<\/em>, Vol.19 (2012)<\/p>\n

\"\"\u00a0No.13\u30002014.7.7
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u5409\u7530\u6587
\n\u8ad6\u6587<\/strong>\uff1aActive Cage Mechanism of Chaperonin-Assisted Protein Folding Demonstrated at Single-Molecule Level
\nAmit J. Gupta et al.
\nJournal of molecular biology<\/em> (2014) in press<\/p>\n

\"\"\u00a0No.12\u30002014.6.30
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u5c0f\u4e95\u5ddd\u6d69\u4e4b
\n\u8ad6\u6587<\/strong>\uff1aSingle-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments
\nAndrea Soranno et al.
\nPNAS<\/em>, vol.111, no.13, 4874-4879<\/p>\n

\"\"\u00a0No.11\u30002014.6.23
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u938c\u5f62\u6e05\u4eba
\n\u8ad6\u6587<\/strong>\uff1aProbing Allostery Through DNA
\nSangjin Kim et al.
\nSCIENCE<\/em>, vol.339<\/p>\n

\"\"\u00a0No.10\u30002014.6.16
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u9ad8\u6a4b\u8061
\n\u8ad6\u6587<\/strong>\uff1aAccounting for a mirror-image congormation as a subtle effect in protein folding
\nKhatuna Kachlishvili et al.
\nPNAS<\/em>, Early Edition<\/p>\n

\"\"\u00a0No.9\u30002014.6.9
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u9ad8\u6a4b\u5f8b\u4e45
\n\u8ad6\u6587<\/strong>\uff1aDigital microfluidic assay for protein detection
\nJanine Mok et al.
\nPNAS<\/em> (2014) 111(6) 2110-2115<\/p>\n

\"\"\u00a0No.8\u30002014.6.2
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u5c0f\u91ce\u5bfa\u967d\u592a\u6717
\n\u8ad6\u6587<\/strong>\uff1aRemodeling of the Folding Free Energy Landscape of Staphylococcal Nuclease by Cavity-Creating Mutantions
\nJulien Roshe et al.
\nBiochemistry<\/em>, (2012) Nov.27 ; 51 (47):9535-46<\/p>\n

\"\"\u00a0No.7\u30002014.5.26
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u4e94\u5341\u5d50\u5343\u88d5
\n\u8ad6\u6587<\/strong>\uff1a One-Pot Synthesis of DNA-CdTe:Zn2+<\/sup> Nanocrystals using Na2<\/sub>TeO3<\/sub> as the Te source
\nCuiling Zhang Ji Yan et al.
\nACS Appl. Mater.Interfaces<\/em> (2014), 6, 3189-3194<\/p>\n

\"\"\u00a0No.6\u30002014.5.19
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u5207\u53e3\u7406\u6075
\n\u8ad6\u6587<\/strong>\uff1aAutomated, high-throughput platform for protein solubility screening using a split-GFP system
\nPawel Listwan et al.
\nJ Struct Funct Genomics<\/em> (2009) 10:47-55<\/p>\n

\"\"\u00a0No.5\u30002014.5.12
\n\u62c5\u5f53\u8005<\/strong>\uff1aDwiky
\n\u8ad6\u6587<\/strong>\uff1aAn infrared reporter to detect spatiotemporal dynamics of protein-protein interactions
\nEmmanuelle Tchekanda et al.
\nNature Methods<\/em> (2014)<\/p>\n

\"\"\u00a0No.4\u30002014.4.28
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u963f\u8607\u88d5\u6a39
\n\u8ad6\u6587<\/strong>\uff1aNano-Analysis fo DNA Conformation Changes Induced by Transcription Factor Complex Binding Using Plasmonic nanodimers
\nhiroyuki Morimura et al.
\nACS NANO<\/em>, vol7. no.12. 10733-10740, 2013<\/p>\n

\"\"\u00a0No.3\u30002014.4.22
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u4f0a\u85e4\u512a\u5fd7
\n\u8ad6\u6587<\/strong>\uff1aProtein analysis by time-resolved measurements with an electro-switchable DNA chip
\nAndreas Langer et al.
\nNature Comunications<\/em>, 2013, DOI:10.1038\/ncomms3099<\/p>\n

\"\"\u00a0No.2\u30002014.4.14
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u6751\u7530\u5d07\u4eba
\n\u8ad6\u6587<\/strong>\uff1aSelf-reproduction of supramolecular giant vesicles combined with the amplification of encapsulated DNA
\nKensuke Kurihara et al.
\nNature Chemistry,<\/em> Vol.3, October 2011, 775-781<\/p>\n

\"\"\u00a0\u00a0No.1\u30002014.4.7
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u9f4a\u85e4\u96c5\u5d69
\n\u8ad6\u6587<\/strong>\uff1aEffect of Internal Cavities on Folding Rates and Routes Revealed by Real-Time Pressure-Jump NMR Spectroscopy
\nJulien Roche et al.
\nJ. Am. Chem. Soc.<\/em> 2013, 135, 14610-14618<\/p>\n","protected":false},"excerpt":{"rendered":"

\u00a0No.36\u30002015.3.16 \u62c5\u5f53\u8005\uff1a\u4f0a\u85e4\u512a\u5fd7 \u8ad6\u6587\uff1aMicrosecond Folding and Domain Mo…<\/p>\n","protected":false},"author":1,"featured_media":0,"parent":151,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-162","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/162","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/comments?post=162"}],"version-history":[{"count":1,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/162\/revisions"}],"predecessor-version":[{"id":163,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/162\/revisions\/163"}],"up":[{"embeddable":true,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/151"}],"wp:attachment":[{"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/media?parent=162"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}