{"id":172,"date":"2015-12-08T15:40:12","date_gmt":"2015-12-08T06:40:12","guid":{"rendered":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/?page_id=172"},"modified":"2015-12-08T15:42:39","modified_gmt":"2015-12-08T06:42:39","slug":"%e8%ab%96%e6%96%87%e7%b4%b9%e4%bb%8b2009","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%8b2009\/","title":{"rendered":"\u8ad6\u6587\u7d39\u4ecb2009"},"content":{"rendered":"

\"\"<\/p>\n

\"\"\u00a0No.27\u30002010.3.19
\n\u62c5\u5f53\u8005\uff1a\u938c\u5f62\u6e05\u4eba
\n\u8ad6\u6587\uff1aProtein folding stability and dynamics imaged in a living cell
\nSimon Ebbinghaus et al.
\nNature Methods, 2010<\/p>\n

\"\"\u00a0No.26\u30002010.2.26
\n\u62c5\u5f53\u8005\uff1a\u9ad8\u6a4b\u8061
\n\u8ad6\u6587\uff1aExperimental evidence for a frustrated energy landscape in a three-helix-bundle protein family
\nBeth G. Wensley et al.
\nNature, 2010,463,685-689<\/p>\n

\"\"\u00a0No.25\u30002010.2.12
\n\u62c5\u5f53\u8005\uff1a\u5c0f\u4e95\u5ddd\u6d69\u4e4b
\n\u8ad6\u6587\uff1aMultiple native states reveal persistent ruggedness of an RNA foldinf landscape
\nsergey V.Solomatin, Max Greenfeld, Steven Chu & Daniel Herschlag
\nNature, 2010,463,681-686<\/p>\n

\"\"\u00a0No.24\u30002010.2.1
\n\u62c5\u5f53\u8005\uff1a\u938c\u5f62\u6e05\u4eba
\n\u8ad6\u6587\uff1aThe role of dynamic conformational ensembles in biomolecular recognition
\nDavid D Boehr, Ruth Nussinov, Peter E Wright
\nNature Chemical Biology 5;789-796 \u00a0(2009)<\/p>\n

\"\"\u00a0No.23\u30002010.1.22
\n\u62c5\u5f53\u8005\uff1a\u9ad8\u6a4b\u8061
\n\u8ad6\u6587\uff1aSingle-molecule denaturation and degradation of proteins by the AAA+ ClpXP protease
\nYongdae Shin et al.
\nProc Natl Acad Sci USA<\/i>,\u00a02009<\/b>, 106, 19340-19345<\/p>\n

\"\"\u00a0No.22\u30002009.12.25
\n\u62c5\u5f53\u8005\uff1a\u5c0f\u4e95\u5ddd\u6d69\u4e4b
\n\u8ad6\u6587\uff1aSingle-molecule spectroscopy of the temperature induced collapse of unfolded protein
\nDaniel Nettels et al.
\nProc Natl Acad Sci USA<\/i>,\u00a02009<\/b>, 106, 20740-20745<\/p>\n

\"\"\u00a0No.21\u30002009.12.11
\n\u62c5\u5f53\u8005\uff1a\u9ad8\u6a4b\u8061
\n\u8ad6\u6587\uff1aExploitation of binding energy for catalysis and design
\nSummer B.Thyme et al.
\nNature 08508 vol 461\/29 October \u00a0(2009)<\/p>\n

\"\"\u00a0No.20\u30002009.11.20
\n\u62c5\u5f53\u8005\uff1a\u938c\u5f62\u6e05\u4eba
\n\u8ad6\u6587\uff1aOrientational averaging of dye molecules attached to proteins in F\u00f6rster resonance energy transfer measurements: insights from a simulation study.
\nAllen LR, Paci E.
\nJ Chem Phys. Aug 14;131(6):065101 (2009)<\/p>\n

\"\"\u00a0No.19\u30002009.11.6
\n\u62c5\u5f53\u8005\uff1a\u5c0f\u4e95\u5ddd\u6d69\u4e4b
\n\u8ad6\u6587\uff1aDirect observation of ultrafast folding and denaturedstate dynamics in single protein molecules
\nHannes Neuweilera, Christopher M. Johnsona and AlanR. Fershta
\nProc Natl Acad Sci USA<\/i>,\u00a02009<\/b>, 106, 18569-18574<\/p>\n

\"\"\u00a0No.18\u30002009.10.16
\n\u62c5\u5f53\u8005\uff1a\u5c71\u68ee\u660e\u5f18
\n\u8ad6\u6587\uff1aLigand Binding Mechanics of Maltose Biding Protein
\nMorten Berts and Matthias Rief
\nJ.Mol.Biol.(2009)<\/p>\n

\"\"\u00a0No.17\u30002009.10.9
\n\u62c5\u5f53\u8005\uff1a\u9ad8\u6a4b\u8061
\n\u8ad6\u6587\uff1aDirect observation of barrier-limited folding of BBL by single-molecule fluorescence resonance energy transfer.
\nFang Huang, Liming Ying, and Alan R.Fersht
\nPNAS(2009),vol.106, 16239-16244<\/p>\n

\"\"\u00a0No.16\u30002009.10.2
\n\u62c5\u5f53\u8005\uff1a\u938c\u5f62\u6e05\u4eba
\n\u8ad6\u6587\uff1aSubdomain-specific collapse of denatured staphylococcal nuclease revealed by single molecule fluorescence resonance energy transfer measurements.
\nPengcheng LIu et al.
\nJ.Phys.Chem.B,113(35),pp12030-12036 (2009)<\/p>\n

\"\"\u00a0No.15\u30002009.9.11
\n\u62c5\u5f53\u8005\uff1a\u5c0f\u4e95\u5ddd\u6d69\u4e4b
\n\u8ad6\u6587\uff1aMicrofluidic Device for Single-Molecule Experiments with Enhanced Photostability
\nEdward A. Lemke et al.
\nJ.Am.Chem.Soc. (2009)<\/p>\n

\"\"\u00a0No.14\u30002009.8.28
\n\u62c5\u5f53\u8005\uff1a\u5c71\u68ee\u660e\u5f18
\n\u8ad6\u6587\uff1aMapping Transient Partial Unfolding by Protein Engineering and Native-State Proteolysis
\nYoungil Chang and Chiwook Park
\nJ Mol Biol (2009) Aug12 (Epub ahead of print)<\/p>\n

\"\"\u00a0No.13\u30002009.8.21
\n\u62c5\u5f53\u8005\uff1a\u9ad8\u6a4b\u8061
\n\u8ad6\u6587\uff1aDirect observation of an ensemble of stable collapsed states in the mechanical folding of ubiquitin
\nSergi Garcia-Manyes et al.
\nPNAS 106,10534-10539(2009)<\/p>\n

\"\"\u00a0No.12\u30002009.8.6
\n\u62c5\u5f53\u8005\uff1a\u938c\u5f62\u6e05\u4eba
\n\u8ad6\u6587\uff1aMapping the structure and comformational movements of proteins with transition metal ion FRET
\nJustin W Taraska et al.
\nNature Methods (2009)6, 532-537<\/p>\n

\"\"\u00a0No.11\u30002009.7.24
\n\u62c5\u5f53\u8005\uff1a\u5c0f\u4e95\u5ddd\u6d69\u4e4b
\n\u8ad6\u6587\uff1aExperimental determination of upper bound for ransition path time in protein folding from single-molecule photon-by-photon trajectories
\nHoi Sung Chung, John M. Louis and Wiliam A.Eaton
\nPNAS, vol.106,11837-11844(2009)<\/p>\n

\"\"\u00a0No.10\u30002009.7.17
\n\u62c5\u5f53\u8005\uff1a\u5c71\u68ee\u660e\u5f18
\n\u8ad6\u6587\uff1aContinuous dissolution of structure during the unfolding of a small protein
\nSantosh Kumar Jhaa, Deepak Dharb, guruswamy Krishnamoorthyc, and Jayant B.Udgaonkar
\nPNAS,vol106,11113-11118 (2009)<\/p>\n

\"\"\u00a0No.9\u30002009.7.10
\n\u62c5\u5f53\u8005\uff1a\u9ad8\u6a4b\u8061
\n\u8ad6\u6587\uff1aA unified model of protein dynamics
\nHans Frauenfelder et al.
\nPNAS, March31(2009) vol.106 135126-135134<\/p>\n

\"\"\u00a0No.8\u30002009.6.26
\n\u62c5\u5f53\u8005\uff1a\u938c\u5f62\u6e05\u4eba
\n\u8ad6\u6587\uff1aSingle-Molecule Protein Unfolding in Solid State Nanopores
\nDavid S.Talaga and Jiali Li
\nJACS (2009)<\/p>\n

\"\"\u00a0No.7\u30002009.6.11
\n\u62c5\u5f53\u8005\uff1a\u5c71\u68ee\u660e\u5f18
\n\u8ad6\u6587\uff1aPosition-Specific Incorporation of Fluorescent Non-nature Amino Acids into Maltose-Binding Protein for Detetion of Ligand Binding by FRET and Fluorescence Quenching
\nIssei Iijima, Tkahiro Hohsaka<\/p>\n

\u62c5\u5f53\u8005\uff1a\u9ad8\u6a4b\u8061
\n\u8ad6\u6587\uff1aChemBioChem 2009, 999-1006 A Reducing and oxidizing System Minimizes Photobleaching and Blinking of Fluorescent Dyes
\nJan Vofelsang et al.
\nAngew.Chem.Int.ed. (2008) 5465-5469<\/p>\n

\"\"\u00a0No.6\u30002009.5.27
\n\u62c5\u5f53\u8005\uff1a\u5c0f\u4e95\u5ddd\u6d69\u4e4b
\n\u8ad6\u6587\uff1aA microfluidic mixing system for single-molecule measurements
\nShawn H et al.
\nRev.Sci.Instrum 80 (2009) 055105<\/p>\n

\"\"\u00a0No.5\u30002009.5.14
\n\u62c5\u5f53\u8005\uff1a\u9ad8\u6a4b\u8061
\n\u8ad6\u6587\uff1aMinicking the folding pathway to improve homology-free protein structure prediction
\nJoe Debartolo et al.
\nProceedings of the National Academy of Sciences (23 February 2009)<\/p>\n

\"\"\u00a0No.4\u30002009.5.8
\n\u62c5\u5f53\u8005\uff1a\u938c\u5f62\u6e05\u4eba
\n\u8ad6\u6587\uff1aContinuous-flow polymerase chain reaction of single-copy DNA in microfluidic microdroplets.
\nSchaeli Y et al
\nAna Chem.(2009) 305-306
\n\u8ad6\u6587\uff1aLigand-dependent equilibrium fluctuations of single calmodulin molecules
\nJunker JP, Ziegler F, Reif M
\nScience (2009) Jan 30,323(5194): 663-667<\/p>\n

\"\"\u00a0No.3\u30002009.5.1
\n\u62c5\u5f53\u8005\uff1a\u5c0f\u4e95\u5ddd\u6d69\u4e4b
\n\u8ad6\u6587\uff1aTree-dimensional, single-molecule fluorescence imaging beyond the diffraction limit by using a double-helix point spread function
\nSri Rama Prasanna Pavani et al.
\nPNAS (2009) 2995-2999<\/p>\n

\"\"\u00a0No.2\u30002009.4.24
\n\u62c5\u5f53\u8005\uff1a\u938c\u5f62\u6e05\u4eba
\n\u8ad6\u6587\uff1aMicrometer-Scale Translation and Monitoring of Individual Nanocars on Glass
\nSaumyakanti Khatua et al.
\nACS Nano (2009)3,(2) 351-356<\/p>\n

\"\"\u00a0No.1\u30002009.4.13
\n\u62c5\u5f53\u8005\uff1a\u9ad8\u6a4b\u8061
\n\u8ad6\u6587\uff1aMeasuring internal friction of an ultrafast-folding protein
\nTroy Cellmer et al.
\nPNAS (2009) 105, 18320-18325<\/p>\n

\"\"<\/p>\n","protected":false},"excerpt":{"rendered":"

\u00a0No.27\u30002010.3.19 \u62c5\u5f53\u8005\uff1a\u938c\u5f62\u6e05\u4eba \u8ad6\u6587\uff1aProtein folding stability and dyn…<\/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-172","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/172","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=172"}],"version-history":[{"count":1,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/172\/revisions"}],"predecessor-version":[{"id":173,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/172\/revisions\/173"}],"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=172"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}