Cited Article: Hummer, G. Water conduction through the hydrophobic channel of a carbon nanotube
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Number of Citing Articles: 3 new records this week (3 in this e-mail)
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Title:
Water-Driven Assembly of Laser Ablation-Induced Au Condensates as Mesomorphic Nano- and Micro-Tubes
Authors:
Huang, CN; Chen, SY; Zheng, YY; Shen, PY
Author Full Names:
Huang, Chang-Ning; Chen, Shuei-Yuan; Zheng, Yuyuan; Shen, Pouyan
Source:
NANOSCALE RESEARCH LETTERS 4 (9): 1064-1072 SEP 2009
Language:
English
Document Type:
Article
Author Keywords:
Gold; Nanocondensates; Nanotubes; Self-assembly; Water
KeyWords Plus:
SURFACE-ENHANCED RAMAN; GOLD NANOPARTICLES; CARBON NANOTUBE; NANOTECHNOLOGY; TEMPERATURE; PARTICLES; CATALYSIS; CLUSTERS; SILVER; SIZE
Abstract:
Reddish Au condensates, predominant atom clusters and minor amount of multiply twinned particles and fcc nanoparticles with internal compressive stress, were produced by pulsed laser ablation on gold target in de-ionized water under a very high power density. Such condensates were self-assembled as lamellae and then nano- to micro-diameter tubes with multiple walls when aged at room temperature in water for up to 40 days. The nano- and micro-tubes have a lamellar- and relaxed fcc-type wall, respectively, both following partial epitaxial relationship with the co-existing multiply twinned nanoparticles. The entangled tubes, being mesomorphic with a large extent of bifurcation, flexibility, opaqueness, and surface-enhanced Raman scattering, may have potential encapsulated and catalytic/label applications in biomedical systems.
Reprint Address:
Shen, PY, Natl Sun Yat Sen Univ, Inst Mat Sci & Engn, Dept Mat & Optoelect Sci, Ctr Nanosci & Nanotechnol, Kaohsiung 80424, Taiwan.
Research Institution addresses:
[Huang, Chang-Ning; Zheng, Yuyuan; Shen, Pouyan] Natl Sun Yat Sen Univ, Inst Mat Sci & Engn, Dept Mat & Optoelect Sci, Ctr Nanosci & Nanotechnol, Kaohsiung 80424, Taiwan; [Chen, Shuei-Yuan] I Shou Univ, Dept Mech & Automat Engn, Kaohsiung, Taiwan
E-mail Address:
pshen@mail.nsysu.edu.tw
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Cited Reference Count:
34
Times Cited:
0
Publisher:
SPRINGER; 233 SPRING ST, NEW YORK, NY 10013 USA
Subject Category:
Nanoscience & Nanotechnology; Materials Science, Multidisciplinary; Physics, Applied
ISSN:
1931-7573
DOI:
10.1007/s11671-009-9359-x
IDS Number:
483ZU
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Title:
Computational Study of a Nanobiosensor: A Single-Walled Carbon Nanotube Functionalized with the Coxsackie-Adenovirus Receptor
Authors:
Johnson, RR; Rego, BJ; Johnson, ATC; Klein, ML
Author Full Names:
Johnson, Robert R.; Rego, Blake Jon; Johnson, A. T. Charlie; Klein, Michael L.
Source:
JOURNAL OF PHYSICAL CHEMISTRY B 113 (34): 11589-11593 AUG 27 2009
Language:
English
Document Type:
Article
KeyWords Plus:
MOLECULAR-DYNAMICS; DNA; PROTEINS; WATER; SIMULATION; MECHANISM; BINDING
Abstract:
Combining single-walled carbon nanotubes (CNT) with biological molecules provides a route to novel nanoscale materials with many promising applications in nanotechnology and nanomedicine. Recent experiments show that CNTs covalently functionalized with the coxsackie-adenovirus receptor (CAR) serve as biosensors capable of specifically recognizing Knob proteins from the adenovirus capsid. These experiments suggest that CAR retains its biologically active form when bound to CNT, but a detailed understanding of the structural changes that occur within CAR after CNT attachment is lacking. To address this, we have performed all-atom classical molecular dynamics (MD) simulations of CAR and the CAR-Knob complex in aqueous solution alone and also when covalently linked to CNT. The MD results show that the CNT damps structural fluctuations in CAR and reduces the internal mobility of the protein. However, CNT induces very little structural deformation and does not affect CAR's ability!
to specifically bind Knob. This MD study verifies that CAR retains its biological functionality when attached to CNT and provides a computational approach to rationalize nanobiosensing devices.
Reprint Address:
Johnson, RR, Univ Penn, Dept Phys & Astron, Philadelphia, PA 19104 USA.
Research Institution addresses:
[Johnson, Robert R.; Johnson, A. T. Charlie] Univ Penn, Dept Phys & Astron, Philadelphia, PA 19104 USA; [Klein, Michael L.] Univ Penn, Dept Chem, Philadelphia, PA 19104 USA; [Rego, Blake Jon] Columbia Univ, Fu Fdn, Sch Engn & Appl Sci, New York, NY 10027 USA
E-mail Address:
robertjo@physics.upenn.edu; cjohnson@physics.upenn.edu
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28
Times Cited:
0
Publisher:
AMER CHEMICAL SOC; 1155 16TH ST, NW, WASHINGTON, DC 20036 USA
Subject Category:
Chemistry, Physical
ISSN:
1520-6106
DOI:
10.1021/jp901999a
IDS Number:
484BI
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Title:
Computational study of the transmembrane domain of the acetylcholine receptor
Authors:
Song, C; Corry, B
Author Full Names:
Song, Chen; Corry, Ben
Source:
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS 38 (7): 961-970 SEP 2009
Language:
English
Document Type:
Article
Author Keywords:
Ion channel; Acetylcholine receptor; Gating; Membrane potential; Molecular dynamics; Brownian dynamics
KeyWords Plus:
GATED ION-CHANNEL; NORMAL-MODE ANALYSIS; PARTICLE MESH EWALD; X-RAY-STRUCTURE; BROWNIAN DYNAMICS; GATING MECHANISM; VOLTAGE-DEPENDENCE; POTASSIUM CHANNEL; SINGLE-CHANNEL; OPEN STATE
Abstract:
The nicotinic acetylcholine receptor (nAChR) is a ligand-gated ion channel protein whose transmembrane domain (TM-domain) is believed to be responsible for channel gating via a hydrophobic effect. In this work, we perform molecular dynamics and Brownian dynamics simulations to investigate the effect of transmembrane potential on the conformation and water occupancy of TM-domain, and the resulting ion permeation events. The results show that the behavior of the hydrophobic gate is voltage-dependent. Large hyperpolarized membrane potential can change the conformation of TM-domain and water occupancy in this region, which may enable ion conduction. An electrostatic gating mechanism is also proposed from our simulations, which seems to play a role in addition to the well-known hydrophobic effect.
Reprint Address:
Song, C, Univ Western Australia, Sch Biomed Biomol & Chem Sci, Crawley, WA 6009, Australia.
Research Institution addresses:
[Song, Chen; Corry, Ben] Univ Western Australia, Sch Biomed Biomol & Chem Sci, Crawley, WA 6009, Australia
E-mail Address:
sc3210@gmail.com
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Cited Reference Count:
47
Times Cited:
0
Publisher:
SPRINGER; 233 SPRING ST, NEW YORK, NY 10013 USA
Subject Category:
Biophysics
ISSN:
0175-7571
DOI:
10.1007/s00249-009-0476-3
IDS Number:
484OK
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