Scanning Force Microscopy Studies of Implanted Silicon Crystals

Lekki, Janusz; Lekka, Małgorzata; Romano, H.; Cleff, B.; Stachura, Z.

doi:10.12693/aphyspola.89.315

Cited by 10 publications

(6 citation statements)

References 8 publications

(13 reference statements)

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“…A home-built atomic force microscope [19] was used to measure the interaction force between proteins. Force-distance curves were recorded at different retraction velocities ranging from 0.2 to 1.7 µm/s.…”

Section: Atomic Force Microscopymentioning

confidence: 99%

Atomic Force Microscopy and Quartz Crystal Microbalance Study of the Lectin-Carbohydrate Interaction Kinetics

et al. 2007

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Two analytical methods, atomic force microscopy and quartz crystal microbalance, were applied to the study of the reaction kinetics occurring between concanavalin A and carboxypeptidase Y, presenting the specific lectin-carbohydrate recognition. The dissociation rate constants for concanavalin A-carboxypeptidase Y complex obtained using both atomic force microscopy and quartz crystal microbalance were of the same order of magnitude: k diss = 0.170 ± 0.060 s −1 and k diss = 0.095 ± 0.002 s −1 , respectively. In addition, each method alone aided in determining other parameters characterizing the studied interaction. Quartz crystal microbalance permitted us to estimate the association rate (k ass = (5.6 ± 0.1) × 10 4 M −1 s −1 ) and the equilibrium (Ka = (0.59 ± 0.01) × 10 6 M −1 ) constants for the binding process occurring between concanavalin A and mannose residues of carboxypeptidase Y under given experimental conditions. Atomic force microscopy in force spectroscopy mode enabled the determination of the energy barrier position of r = 2.29 ± 0.04Å characterizing the dissociation of concanavalin Acarboxypeptidase Y molecular complex. The presented results show that both atomic force microscopy and quartz crystal microbalance can be used to determine quantitative parameters characterizing the specific molecular interaction. Both methods can be easily combined for complementary and/or alternative studies of a chosen molecular interaction. By preparing the samples in the same manner the direct comparison between the data obtained via atomic force microscopy and quartz crystal microbalance can be made.

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Section: Atomic Force Microscopymentioning

confidence: 99%

Atomic Force Microscopy and Quartz Crystal Microbalance Study of the Lectin-Carbohydrate Interaction Kinetics

et al. 2007

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“…The topography of Con A-modified surfaces was measured using a homemade atomic force microscope [34], working in contact mode. Commercially available silicon nitride cantilevers with a spring constant of 0.01 N/m (Veeco) were used for imaging.…”

Section: Atomic Force Microscopy (Afm)mentioning

confidence: 99%

Lectin–carbohydrate affinity measured using a quartz crystal microbalance

Lebed¹,

Kulik²,

Forró³

et al. 2006

Journal of Colloid and Interface Science

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“…Surface topography formed in the course of spin-casting was examined by AFM working in contact mode. Images were recorded in air at room temperature 29,59 with the home-built 57 AFM apparatus 59 and with CP Park Scientific Instruments AFM microscope. 29 Film thickness 〈h〉 was determined from AFM images taken after partial removal of the polymer film by a scalpel scratch.…”

Section: Characterization Of Polymer Blendmentioning

confidence: 99%

Structures Formed in Spin-Cast Films of Polystyrene Blends with Poly(butyl methacrylate) Isomers

et al. 2004

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For polystyrene blends with poly(butyl methacrylate), replacing poly(n-butyl methacrylate) by poly(tert-butyl methacrylate) results in modified topography of spin-cast films (holes dominating at a surface are exchanged with islands, or vice versa, such individual surface features are increased), decreased PBMA surface excess, but similar overall domain structure. Two series (PS/PnBMA and PS/PtBMA) of films with constant thickness and PBMA fraction 0 < Φ < 1, cast from toluene onto silicon wafers, were examined with atomic force microscopy, X-ray photoelectron spectroscopy, profiling and mapping mode of dynamic secondary ion mass spectrometry. Topography was analyzed with the integral geometry approach. Film structure formation was postulated to involve surface segregation, phase separation, and instability of the transient PBMA layer [a linear relation between Φ2 and averaged size of holes (islands) was observed for PS/PnBMA (PS/PtBMA)]. Structural changes caused by isomer exchange are related to glass transition temperature and blend incompatibility; both increased for PtBMA.

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Scanning Force Microscopy Studies of Implanted Silicon Crystals

Cited by 10 publications

References 8 publications

Atomic Force Microscopy and Quartz Crystal Microbalance Study of the Lectin-Carbohydrate Interaction Kinetics

Atomic Force Microscopy and Quartz Crystal Microbalance Study of the Lectin-Carbohydrate Interaction Kinetics

Lectin–carbohydrate affinity measured using a quartz crystal microbalance

Structures Formed in Spin-Cast Films of Polystyrene Blends with Poly(butyl methacrylate) Isomers

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