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  • 1
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    DNA: a programmable force sensor (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-07-19
    Description: Direct quantification of biomolecular interaction by single-molecule force spectroscopy has evolved into a powerful tool for materials and life sciences. We introduce an approach in which the unbinding forces required to break intermolecular bonds are measured in a differential format by comparison with a known reference bond (here, a short DNA duplex). In addition to a marked increase in sensitivity and force resolution, which enabled us to resolve single-base pair mismatches, this concept allows for highly specific parallel assays. This option was exploited to overcome cross-reactions of antibodies in a protein biochip application.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Albrecht, Christian -- Blank, Kerstin -- Lalic-Multhaler, Mio -- Hirler, Siegfried -- Mai, Thao -- Gilbert, Ilka -- Schiffmann, Susanne -- Bayer, Tom -- Clausen-Schaumann, Hauke -- Gaub, Hermann E -- New York, N.Y. -- Science. 2003 Jul 18;301(5631):367-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nanotype GmbH, Lochhamer Schlag 12, 82166 Grafelfing, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12869761" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies ; *Base Pair Mismatch ; *Biosensing Techniques ; Carbocyanines ; Cross Reactions ; *DNA/chemistry/genetics/metabolism ; Dimethylpolysiloxanes ; Fluorescence ; Fluorescent Dyes ; Glass ; Humans ; Immunoassay ; Interleukin-5/analysis/immunology ; Mice ; Microscopy, Atomic Force ; Nucleic Acid Conformation ; Nucleic Acid Hybridization ; Oligodeoxyribonucleotides/chemistry/metabolism ; *Oligonucleotide Array Sequence Analysis ; *Protein Array Analysis ; Protein Binding ; Silicones ; Temperature ; Thermodynamics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Unfolding pathways of individual bacteriorhodopsins (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-02-07
    Description: Atomic force microscopy and single-molecule force spectroscopy were combined to image and manipulate purple membrane patches from Halobacterium salinarum. Individual bacteriorhodopsin molecules were first localized and then extracted from the membrane; the remaining vacancies were imaged again. Anchoring forces between 100 and 200 piconewtons for the different helices were found. Upon extraction, the helices were found to unfold. The force spectra revealed the individuality of the unfolding pathways. Helices G and F as well as helices E and D always unfolded pairwise, whereas helices B and C occasionally unfolded one after the other. Experiments with cleaved loops revealed the origin of the individuality: stabilization of helix B by neighboring helices.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oesterhelt, F -- Oesterhelt, D -- Pfeiffer, M -- Engel, A -- Gaub, H E -- Muller, D J -- New York, N.Y. -- Science. 2000 Apr 7;288(5463):143-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CeNS and Lehrstuhl fur angewandte Physik, Ludwig Maximilians-Universitat Munchen, Amalienstrasse 54, 80799 Munchen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10753119" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacteriorhodopsins/*chemistry/genetics ; Cysteine/chemistry ; Halobacterium salinarum/*chemistry ; Membrane Proteins/*chemistry/genetics ; *Microscopy, Atomic Force ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Conformation ; Protein Denaturation ; *Protein Folding ; Protein Structure, Secondary ; Purple Membrane/*chemistry ; Serine Endopeptidases/metabolism ; Spectrum Analysis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    How strong is a covalent bond? (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-03-12
    Description: The rupture force of single covalent bonds under an external load was measured with an atomic force microscope (AFM). Single polysaccharide molecules were covalently anchored between a surface and an AFM tip and then stretched until they became detached. By using different surface chemistries for the attachment, it was found that the silicon-carbon bond ruptured at 2.0 +/- 0.3 nanonewtons, whereas the sulfur-gold anchor ruptured at 1.4 +/- 0.3 nanonewtons at force-loading rates of 10 nanonewtons per second. Bond rupture probability calculations that were based on density functional theory corroborate the measured values.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grandbois -- Beyer -- Rief -- Clausen-Schaumann -- Gaub -- New York, N.Y. -- Science. 1999 Mar 12;283(5408):1727-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lehrstuhl fur Angewandte Physik, Ludwig-Maximilians-Universitat, Amalienstrasse 54, D-80799 Munchen, Germany. Institut fur Physikalische und Theoretische Chemie, Technische Universitat Munchen, Lichtenbergstrasse 4, 85748 Garching.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10073936" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
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  • 4
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    Single Molecule Force Spectroscopy on Polysaccharides by Atomic Force Microscopy (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-02-28
    Description: Recent developments in piconewton instrumentation allow the manipulation of single molecules and measurements of intermolecular as well as intramolecular forces. Dextran filaments linked to a gold surface were probed with the atomic force microscope tip by vertical stretching. At low forces the deformation of dextran was found to be dominated by entropic forces and can be described by the Langevin function with a 6 angstrom Kuhn length. At elevated forces the strand elongation was governed by a twist of bond angles. At higher forces the dextran filaments underwent a distinct conformational change. The polymer stiffened and the segment elasticity was dominated by the bending of bond angles. The conformational change was found to be reversible and was corroborated by molecular dynamics calculations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rief -- Oesterhelt -- Heymann -- Gaub -- New York, N.Y. -- Science. 1997 Feb 28;275(5304):1295-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉M. Rief, F. Oesterhelt, H. E. Gaub, Lehrstuhl fur Angewandte Physik, Ludwig-Maximilians-Universitat, 80799 Munchen, Germany. B. Heymann, Theoretische Biophysik, Institut fur Medizinische Optik, Ludwig-Maximilians-Universitat 80333 Munchen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9036852" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    From molecules to cells: imaging soft samples with the atomic force microscope (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-09-25
    Description: Since its invention a few years ago, the atomic force microscope has become one of the most widely used near-field microscopes. Surfaces of hard sample are imaged routinely with atomic resolution. Soft samples, however, remain challenging. An overview is presented on the application of atomic force microscopy to organic samples ranging from thin ordered films at molecular resolution to living cells. Fundamental mechanisms of the image formation are discussed, and novel imaging modes are introduced that exploit different aspects of the tip-sample interaction for local measurements of the micromechanical properties of the sample. As examples, images of Langmuir-Blodgett films, which map the local viscoelasticity as well as the friction coefficient, are presented.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Radmacher, M -- Tillamnn, R W -- Fritz, M -- Gaub, H E -- New York, N.Y. -- Science. 1992 Sep 25;257(5078):1900-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Physikdepartment, Technische Universitat Munchen, 8046 Garching, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411505" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/ultrastructure ; Amino Acids ; Blood Platelets/cytology ; Crystallography ; Elasticity ; Humans ; Microscopy/*instrumentation ; Platelet Activation ; Proteins/ultrastructure ; Viscosity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 6
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    Reversible unfolding of individual titin immunoglobulin domains by AFM (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-16
    Description: Single-molecule atomic force microscopy (AFM) was used to investigate the mechanical properties of titin, the giant sarcomeric protein of striated muscle. Individual titin molecules were repeatedly stretched, and the applied force was recorded as a function of the elongation. At large extensions, the restoring force exhibited a sawtoothlike pattern, with a periodicity that varied between 25 and 28 nanometers. Measurements of recombinant titin immunoglobulin segments of two different lengths exhibited the same pattern and allowed attribution of the discontinuities to the unfolding of individual immunoglobulin domains. The forces required to unfold individual domains ranged from 150 to 300 piconewtons and depended on the pulling speed. Upon relaxation, refolding of immunoglobulin domains was observed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rief, M -- Gautel, M -- Oesterhelt, F -- Fernandez, J M -- Gaub, H E -- New York, N.Y. -- Science. 1997 May 16;276(5315):1109-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lehrstuhl fur Angewandte Physik, Munchen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9148804" target="_blank"〉PubMed〈/a〉
    Keywords: Adsorption ; Connectin ; Elasticity ; Entropy ; Immunoglobulins/*chemistry ; Microscopy, Atomic Force ; Monte Carlo Method ; Muscle Proteins/*chemistry ; *Protein Folding ; Protein Kinases/*chemistry ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry ; Stress, Mechanical ; Thermodynamics
    Print ISSN: 0036-8075
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  • 7
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    Single-molecule optomechanical cycle (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-05-11
    Description: Light-powered molecular machines are conjectured to be essential constituents of future nanoscale devices. As a model for such systems, we have synthesized a polymer of bistable photosensitive azobenzenes. Individual polymers were investigated by single-molecule force spectroscopy in combination with optical excitation in total internal reflection. We were able to optically lengthen and contract individual polymers by switching the azo groups between their trans and cis configurations. The polymer was found to contract against an external force acting along the polymer backbone, thus delivering mechanical work. As a proof of principle, the polymer was operated in a periodic mode, demonstrating for the first time optomechanical energy conversion in a single-molecule device.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hugel, Thorsten -- Holland, Nolan B -- Cattani, Anna -- Moroder, Luis -- Seitz, Markus -- Gaub, Hermann E -- New York, N.Y. -- Science. 2002 May 10;296(5570):1103-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lehrstuhl fur Angewandte Physik & Center for Nanoscience, Ludwig-Maximilians Universitat, Amalienstrasse 54, 80799 Munchen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004125" target="_blank"〉PubMed〈/a〉
    Keywords: Azo Compounds/*chemistry ; Chemistry, Physical ; Dimethyl Sulfoxide ; *Light ; Mechanics ; Microscopy, Atomic Force ; Molecular Conformation ; Nanotechnology ; Optics and Photonics ; Peptides/*chemistry ; Photochemistry ; Physicochemical Phenomena ; Polymers ; Protein Conformation ; Software ; Spectrum Analysis ; Temperature
    Print ISSN: 0036-8075
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  • 8
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    Fibrous mini-collagens in hydra nematocysts (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-15
    Description: Nematocysts (cnidocysts) are exocytotic organelles found in all cnidarians. Here, atomic force microscopy and field emission scanning electron microscopy reveal the structure of the nematocyst capsule wall. The outer wall consists of globular proteins of unknown function. The inner wall consists of bundles of collagen-like fibrils having a spacing of 50 to 100 nanometers and cross-striations at intervals of 32 nanometers. The fibrils consist of polymers of "mini-collagens," which are abundant in the nematocysts of Hydra. The distinct pattern of mini-collagen fibers in the inner wall can provide the tensile strength necessary to withstand the high osmotic pressure (15 megapascals) in the capsules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holstein, T W -- Benoit, M -- Herder, G V -- David, C N -- Wanner, G -- Gaub, H E -- New York, N.Y. -- Science. 1994 Jul 15;265(5170):402-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17838043" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
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  • 9
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    Adhesion forces between individual ligand-receptor pairs (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-15
    Description: The adhesion force between the tip of an atomic force microscope cantilever derivatized with avidin and agarose beads functionalized with biotin, desthiobiotin, or iminobiotin was measured. Under conditions that allowed only a limited number of molecular pairs to interact, the force required to separate tip and bead was found to be quantized in integer multiples of 160 +/- 20 piconewtons for biotin and 85 +/- 15 piconewtons for iminobiotin. The measured force quanta are interpreted as the unbinding forces of individual molecular pairs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Florin, E L -- Moy, V T -- Gaub, H E -- New York, N.Y. -- Science. 1994 Apr 15;264(5157):415-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Physikdepartment der Technischen Universitat Munchen, Garching, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8153628" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesiveness ; Avidin/*chemistry ; Biotin/analogs & derivatives/*chemistry ; Ligands ; Microscopy/methods ; Microspheres ; Receptors, Cell Surface/*chemistry ; Sepharose
    Print ISSN: 0036-8075
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  • 10
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    Intermolecular forces and energies between ligands and receptors (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-14
    Description: The recognition mechanisms and dissociation pathways of the avidin-biotin complex and of actin monomers in actin filaments were investigated. The unbinding forces of discrete complexes of avidin or streptavidin with biotin analogs are proportional to the enthalpy change of the complex formation but independent of changes in the free energy. This result indicates that the unbinding process is adiabatic and that entropic changes occur after unbinding. On the basis of the measured forces and binding energies, an effective rupture length of 9.5 +/- 1 angstroms was calculated for all biotin-avidin pairs and approximately 1 to 3 angstroms for the actin monomer-monomer interaction. A model for the correlation among binding forces, intermolecular potential, and molecular function is proposed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moy, V T -- Florin, E L -- Gaub, H E -- New York, N.Y. -- Science. 1994 Oct 14;266(5183):257-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, Technische Universitat Munchen, Garching, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939660" target="_blank"〉PubMed〈/a〉
    Keywords: Avidin/*chemistry/metabolism ; Bacterial Proteins/chemistry/metabolism ; Biotin/analogs & derivatives/*chemistry/metabolism ; Hydrogen-Ion Concentration ; *Ligands ; Models, Chemical ; Receptors, Drug/*chemistry ; Streptavidin ; Thermodynamics
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