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5 Sep 2005

Volume 87, Issue 10, Articles (10xxxx)

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Appl. Phys. Lett. 87, 101107 (2005); http://dx.doi.org/10.1063/1.2039987 (3 pages)

A. David, C. Meier, R. Sharma, F. S. Diana, S. P. DenBaars, E. Hu, S. Nakamura, C. Weisbuch, and H. Benisty
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Free-standing protein films for dynamic mode detection of cations binding

Daisuke Saya, Anthony W. Coleman, Adina N. Lazar, Christian Bergaud, and Liviu Nicu

Appl. Phys. Lett. 87, 103901 (2005); http://dx.doi.org/10.1063/1.2035872 (3 pages)

Online Publication Date: 29 August 2005

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This letter reports on the investigation of the mechano-chemical effect of cross-linked dried free-standing alpha-lactalbumin (α-lactalbumin) thin films induced by different cation, calcium, magnesium, and potassium binding. The protein membranes were fabricated by drying droplets of an α-lactalbumin solution on top of silicon through-wafer holes obtained by deep reactive ion etching. Then the membranes were consecutively exposed to solutions of the cations in HEPES buffer solution while their resonant frequencies were measured by full-field surface stroboscopic white light interferometry. Tests on more than 30 free-standing protein films showed more significant conformational changes of the α-lactalbumin after immersion in a calcium solution than those observed after immersion in magnesium and potassium solutions. These results demonstrate, the real potential of free-standing protein films to be used as resonant biosensors for multiple cation detection.
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87.80.-y Biophysical techniques (research methods)
87.15.H- Dynamics of biomolecules
87.15.La Mechanical properties
87.15.N- Properties of solutions of macromolecules
36.20.Ey Conformation (statistics and dynamics)
87.14.E- Proteins

Prediction of protein crystallization based on interfacial and diffusion kinetics

Yanwei Jia and Xiang-Yang Liu

Appl. Phys. Lett. 87, 103902 (2005); http://dx.doi.org/10.1063/1.2040006 (3 pages)

Online Publication Date: 31 August 2005

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The interfacial kinetics of protein crystallization was studied via the kinetics of protein two-dimensional self-assembly. The competition between the protein volume transport and surface integration determines whether single crystals or amorphous aggregation will occur. A kinetic coefficient was found to provide an effective and reliable criterion to predict protein crystallization conditions. This criterion has been applied to lysozyme, concanavalin A and BSA crystallization, and it turned out to be very successful and more reliable than the second virial coefficient criterion.
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87.15.N- Properties of solutions of macromolecules
87.15.Vv Diffusion
87.14.E- Proteins

Characteristics of field-effect devices with gate oxide modification by DNA

G. Xuan, J. Kolodzey, V. Kapoor, and G. Gonye

Appl. Phys. Lett. 87, 103903 (2005); http://dx.doi.org/10.1063/1.2041826 (3 pages) | Cited 7 times

Online Publication Date: 31 August 2005

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Current-voltage characterization was used to investigate the behavior of silicon field-effect devices with DNA solutions of various concentrations and molecular states deposited on the gate oxide. These devices were similar to conventional transistors but without gate metal, and no surface treatments or agents were used to immobilize the DNA. With increasing micromolar concentration, significant changes were produced in the device response. The current decreased with increasing ratios of double-to-single stranded populations produced by mixing complementary sequences, and by thermal denaturing. The device characteristics were reproducible. Modeling suggested a mechanism of modifications to the device carrier density induced by variations in the electrochemical properties of the DNA located within a charge screening length of the gate oxide surface. These results showed that field-effect devices may be useful for the real time monitoring of nucleic acids, without binding agents or label tags.
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87.80.-y Biophysical techniques (research methods)
85.30.Tv Field effect devices
85.30.De Semiconductor-device characterization, design, and modeling
87.15.N- Properties of solutions of macromolecules
87.14.G- Nucleic acids
82.45.Tv Bioelectrochemistry
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