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  • Cell & Developmental Biology
  • Elasticity
  • Inorganic Chemistry
  • LUNAR AND PLANETARY EXPLORATION
  • American Association for the Advancement of Science (AAAS)  (9)
  • 2000-2004  (9)
  • 1
    Publication Date: 2004-05-29
    Description: Networks of cross-linked and bundled actin filaments are ubiquitous in the cellular cytoskeleton, but their elasticity remains poorly understood. We show that these networks exhibit exceptional elastic behavior that reflects the mechanical properties of individual filaments. There are two distinct regimes of elasticity, one reflecting bending of single filaments and a second reflecting stretching of entropic fluctuations of filament length. The mechanical stiffness can vary by several decades with small changes in cross-link concentration, and can increase markedly upon application of external stress. We parameterize the full range of behavior in a state diagram and elucidate its origin with a robust model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gardel, M L -- Shin, J H -- MacKintosh, F C -- Mahadevan, L -- Matsudaira, P -- Weitz, D A -- GM52703/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 May 28;304(5675):1301-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15166374" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*chemistry/metabolism ; Actins/*chemistry/metabolism ; Biopolymers/chemistry/metabolism ; Elasticity ; Entropy ; Mathematics ; Microfilament Proteins/chemistry/metabolism ; Models, Biological ; Stress, Mechanical
    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
    Publication Date: 2002-04-27
    Description: The introduction of biodegradable implant materials as well as minimally invasive surgical procedures in medicine has substantially improved health care within the past few decades. This report describes a group of degradable thermoplastic polymers that are able to change their shape after an increase in temperature. Their shape-memory capability enables bulky implants to be placed in the body through small incisions or to perform complex mechanical deformations automatically. A smart degradable suture was created to illustrate the potential of these shape-memory thermoplastics in biomedical applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lendlein, Andreas -- Langer, Robert -- New York, N.Y. -- Science. 2002 May 31;296(5573):1673-6. Epub 2002 Apr 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉mnemoScience GmbH, Pauwelsstrabetae 19, D-52074 Aachen, Germany. a.lendlein@mnemoscience.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11976407" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biocompatible Materials/chemical synthesis/chemistry ; Chemistry, Physical ; Dioxanes/chemistry ; Elasticity ; Elastomers ; Isocyanates/chemistry ; Mechanics ; Physicochemical Phenomena ; Polyesters/chemistry ; *Polymers/chemical synthesis/chemistry ; *Prostheses and Implants ; Rats ; Stress, Mechanical ; *Sutures ; 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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  • 3
    Publication Date: 2002-01-19
    Description: Spider silks are protein-based "biopolymer" filaments or threads secreted by specialized epithelial cells as concentrated soluble precursors of highly repetitive primary sequences. Spider dragline silk is a flexible, lightweight fiber of extraordinary strength and toughness comparable to that of synthetic high-performance fibers. We sought to "biomimic" the process of spider silk production by expressing in mammalian cells the dragline silk genes (ADF-3/MaSpII and MaSpI) of two spider species. We produced soluble recombinant (rc)-dragline silk proteins with molecular masses of 60 to 140 kilodaltons. We demonstrated the wet spinning of silk monofilaments spun from a concentrated aqueous solution of soluble rc-spider silk protein (ADF-3; 60 kilodaltons) under modest shear and coagulation conditions. The spun fibers were water insoluble with a fine diameter (10 to 40 micrometers) and exhibited toughness and modulus values comparable to those of native dragline silks but with lower tenacity. Dope solutions with rc-silk protein concentrations 〉20% and postspinning draw were necessary to achieve improved mechanical properties of the spun fibers. Fiber properties correlated with finer fiber diameter and increased birefringence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lazaris, Anthoula -- Arcidiacono, Steven -- Huang, Yue -- Zhou, Jiang-Feng -- Duguay, Francois -- Chretien, Nathalie -- Welsh, Elizabeth A -- Soares, Jason W -- Karatzas, Costas N -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):472-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nexia Biotechnologies, Vaudreuil-Dorion, Quebec J7V 8P5, Canada. alazaris@nexiabiotech.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799236" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Biopolymers ; Birefringence ; Cattle ; Cell Line ; Cloning, Molecular ; Cricetinae ; Culture Media, Conditioned ; DNA, Complementary ; Elasticity ; Epithelial Cells/metabolism ; *Fibroins ; Materials Testing ; Mechanics ; Molecular Sequence Data ; Molecular Weight ; *Protein Biosynthesis ; Protein Structure, Secondary ; Proteins/chemistry/*genetics/isolation & purification ; Recombinant Proteins/biosynthesis/chemistry/isolation & purification ; Solubility ; Spiders/*genetics/metabolism ; Stress, Mechanical ; Tensile Strength ; Water
    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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  • 4
    Publication Date: 2002-11-02
    Description: We present an approach to fabricate solid capsules with precise control of size, permeability, mechanical strength, and compatibility. The capsules are fabricated by the self-assembly of colloidal particles onto the interface of emulsion droplets. After the particles are locked together to form elastic shells, the emulsion droplets are transferred to a fresh continuous-phase fluid that is the same as that inside the droplets. The resultant structures, which we call "colloidosomes," are hollow, elastic shells whose permeability and elasticity can be precisely controlled. The generality and robustness of these structures and their potential for cellular immunoisolation are demonstrated by the use of a variety of solvents, particles, and contents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dinsmore, A D -- Hsu, Ming F -- Nikolaides, M G -- Marquez, Manuel -- Bausch, A R -- Weitz, D A -- New York, N.Y. -- Science. 2002 Nov 1;298(5595):1006-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics and DEAS, Harvard University, Cambridge, MA 02138, USA. dinsmore@physics.umass.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12411700" target="_blank"〉PubMed〈/a〉
    Keywords: Adsorption ; *Capsules ; Cell Physiological Phenomena ; Cell Survival ; Cells, Cultured ; Chemistry, Physical ; *Colloids ; Diffusion ; Elasticity ; Emulsions ; Fibroblasts/physiology ; Microscopy, Confocal ; Microscopy, Electron, Scanning ; Permeability ; Physicochemical Phenomena ; Polylysine ; Polymethyl Methacrylate ; Surface Properties ; Water
    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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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-07-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alper, Joe -- New York, N.Y. -- Science. 2002 Jul 19;297(5580):329-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12130765" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Chemistry, Physical ; Collagen/chemistry ; Elasticity ; Elastin/chemistry ; *Fibroins ; Insect Proteins/chemistry ; Microfilament Proteins/chemistry ; Physicochemical Phenomena ; Polymers/*chemistry ; *Protein Conformation ; *Protein Engineering ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/*chemistry ; Recombinant Proteins/chemistry ; Repetitive Sequences, Amino Acid ; Stress, Mechanical
    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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  • 6
    Publication Date: 2001-02-07
    Description: Soft lithography is an alternative to silicon-based micromachining that uses replica molding of nontraditional elastomeric materials to fabricate stamps and microfluidic channels. We describe here an extension to the soft lithography paradigm, multilayer soft lithography, with which devices consisting of multiple layers may be fabricated from soft materials. We used this technique to build active microfluidic systems containing on-off valves, switching valves, and pumps entirely out of elastomer. The softness of these materials allows the device areas to be reduced by more than two orders of magnitude compared with silicon-based devices. The other advantages of soft lithography, such as rapid prototyping, ease of fabrication, and biocompatibility, are retained.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Unger, M A -- Chou, H P -- Thorsen, T -- Scherer, A -- Quake, S R -- DA-9121/DA/NIDA NIH HHS/ -- NS-11756/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2000 Apr 7;288(5463):113-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Applied Physics, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10753110" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesiveness ; *Biocompatible Materials ; Elasticity ; Materials Testing ; Pressure ; *Prostheses and Implants ; *Silicone Elastomers
    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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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-05-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fernandez, J M -- Chu, S -- Oberhauser, A F -- New York, N.Y. -- Science. 2001 Apr 27;292(5517):653-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, Mayo Foundation, Rochester, MN 55905, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11330326" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; Elasticity ; Ion Channels/chemistry ; Kinetics ; *Nucleic Acid Conformation ; Physicochemical Phenomena ; RNA/*chemistry ; RNA Stability ; RNA, Catalytic/*chemistry ; Stress, Mechanical ; 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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  • 8
    Publication Date: 2001-02-07
    Description: The motility of kinesin motors is explained by a "hand-over-hand" model in which two heads of kinesin alternately repeat single-headed and double-headed binding with a microtubule. To investigate the binding mode of kinesin at the key nucleotide states during adenosine 5'-triphosphate (ATP) hydrolysis, we measured the mechanical properties of a single kinesin-microtubule complex by applying an external load with optical tweezers. Both the unbinding force and the elastic modulus in solutions containing AMP-PNP (an ATP analog) were twice the value of those in nucleotide-free solution or in the presence of both AMP-PNP and adenosine 5'-diphosphate. Thus, kinesin binds through two heads in the former and one head in the latter two states, which supports a major prediction of the hand-over-hand model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawaguchi, K -- Ishiwata, S -- New York, N.Y. -- Science. 2001 Jan 26;291(5504):667-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, School of Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11158681" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/*metabolism ; Adenosine Triphosphate/metabolism ; Adenylyl Imidodiphosphate/*metabolism ; Animals ; Cattle ; Elasticity ; Kinesin/*metabolism ; Kinetics ; Microtubules/metabolism ; Models, Biological ; Swine
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-09-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weiss, G -- New York, N.Y. -- Science. 2001 Sep 7;293(5536):1753-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11546850" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cooking ; Elasticity ; Fats/metabolism ; *Food ; Food Analysis ; *Food Preferences/physiology/psychology ; Hot Temperature ; Humans ; Perception ; *Research ; *Sensation ; Smell ; Taste ; Viscosity
    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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