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  • Physicochemical Phenomena  (2)
  • American Association for the Advancement of Science (AAAS)  (2)
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  • American Association for the Advancement of Science (AAAS)  (2)
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  • 1
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    Reproducible measurement of single-molecule conductivity (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-10-20
    Description: A reliable method has been developed for making through-bond electrical contacts to molecules. Current-voltage curves are quantized as integer multiples of one fundamental curve, an observation used to identify single-molecule contacts. The resistance of a single octanedithiol molecule was 900 +/- 50 megohms, based on measurements on more than 1000 single molecules. In contrast, nonbonded contacts to octanethiol monolayers were at least four orders of magnitude more resistive, less reproducible, and had a different voltage dependence, demonstrating that the measurement of intrinsic molecular properties requires chemically bonded contacts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cui, X D -- Primak, A -- Zarate, X -- Tomfohr, J -- Sankey, O F -- Moore, A L -- Moore, T A -- Gust, D -- Harris, G -- Lindsay, S M -- New York, N.Y. -- Science. 2001 Oct 19;294(5542):571-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics and Astronomy, Arizona State University, Tempe, AZ 85287, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11641492" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; *Electric Conductivity ; Electrochemistry ; Gold ; Microscopy, Scanning Tunneling ; Physicochemical Phenomena ; Reproducibility of Results ; Sulfhydryl Compounds/*chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-06-17
    Description: Protein dynamics are essential for protein function, and yet it has been challenging to access the underlying atomic motions in solution on nanosecond-to-microsecond time scales. We present a structural ensemble of ubiquitin, refined against residual dipolar couplings (RDCs), comprising solution dynamics up to microseconds. The ensemble covers the complete structural heterogeneity observed in 46 ubiquitin crystal structures, most of which are complexes with other proteins. Conformational selection, rather than induced-fit motion, thus suffices to explain the molecular recognition dynamics of ubiquitin. Marked correlations are seen between the flexibility of the ensemble and contacts formed in ubiquitin complexes. A large part of the solution dynamics is concentrated in one concerted mode, which accounts for most of ubiquitin's molecular recognition heterogeneity and ensures a low entropic complex formation cost.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lange, Oliver F -- Lakomek, Nils-Alexander -- Fares, Christophe -- Schroder, Gunnar F -- Walter, Korvin F A -- Becker, Stefan -- Meiler, Jens -- Grubmuller, Helmut -- Griesinger, Christian -- de Groot, Bert L -- New York, N.Y. -- Science. 2008 Jun 13;320(5882):1471-5. doi: 10.1126/science.1157092.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Theoretical and Computational Biophysics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18556554" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Animals ; Anisotropy ; Chemistry, Physical ; Crystallography, X-Ray ; Entropy ; Kinetics ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Physicochemical Phenomena ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Solutions ; Ubiquitin/*chemistry/*metabolism ; Xenopus laevis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
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