A new quantitative optical biosensor for protein characterisation

Cross, Graham H.; Reeves, Andrew A.; Brand, S.; Popplewell, Jonathan; Peel, Louise L; Swann, Marcus J.; Freeman, Neville J.

doi:10.1016/s0956-5663(03)00203-3

Cited by 206 publications

(181 citation statements)

References 15 publications

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“…The thickness obtained agrees with the expected dimension of a layer of SspB dimers, placed on their sides, on top of the ZBD dimers (Fig. 13C Upper) (5,16,18). The weak association reaction had a K d of 11.0 M (SspB 2 to ZBD 2 ) and a final thickness of 7.6 nm (Figs.…”

Section: Sspb C Terminus Binds a Hydrophobic Patch On The Surface Of supporting

confidence: 82%

“…2B and data not shown). The NH chemical shift of Phe 16 did not significantly change upon addition of SspB peptide or SspB 2 protein, which is probably because this residue is part of the dimer interface (5); however, Phe 16 is next to Cys 17 , which did show a ⌬␦ av Ͼ400 Hz in Fig. 2B.…”

Section: Sspb C Terminus Binds a Hydrophobic Patch On The Surface Of mentioning

confidence: 88%

“…ITC experiments were performed by using a Microcal (Amherst, MA) VP-ITC and were repeated three times. Other binding experiments were performed by using an AnaLight Bio200 dual waveguide interferometer instrument from Farfield (16). Experiments were performed in buffer D at a flow rate of 0.05 ml͞min.…”

Section: Methodsmentioning

confidence: 99%

“…A further understanding of the mode of interaction of SspB 2 and SspB 154 -165 to ZBD 2 was gained by using an AnaLight Bio200 (Farfield Scientific, Crewe, U.K.) instrument that uses a dual polarization interferometry detection method (16,17). The instrument gives absolute measurements of thickness and density of crosslinked and bound biological molecules on films, with resolution levels of subpicogram per mm 2 and subAngstrom, respectively.…”

Section: Sspb C Terminus Binds a Hydrophobic Patch On The Surface Of mentioning

confidence: 99%

See 3 more Smart Citations

Specificity in substrate and cofactor recognition by the N-terminal domain of the chaperone ClpX

Thibault

Yudin²,

Wong³

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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Clp ATPases are a unique group of ATP-dependent chaperones supporting targeted protein unfolding and degradation in concert with their respective proteases. ClpX is a representative member of these ATPases; it consists of two domains, a zinc-binding domain (ZBD) that forms dimers and a AAA ؉ ATP-binding domain that arranges into a hexamer. Analysis of the binding preferences of these two domains in ClpX revealed that both domains preferentially bind to hydrophobic residues but have different sequence preferences, with the AAA ؉ domain preferentially recognizing a wider range of specific sequences than ZBD. As part of this analysis, the binding site of the ClpX dimeric cofactor, SspB 2, on ZBD in ClpX was determined by NMR and mutational analysis. The SspB C terminus was found to interact with a hydrophobic patch on the surface of ZBD. The affinity of SspB 2 toward ZBD2 and the geometry of the SspB 2-ZBD2 complex were investigated by using the newly developed quantitative optical biosensor method of dual polarization interferometry. The data suggest a model for the interaction between SspB 2 and the ClpX hexamer.

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Section: Sspb C Terminus Binds a Hydrophobic Patch On The Surface Of supporting

confidence: 82%

Section: Sspb C Terminus Binds a Hydrophobic Patch On The Surface Of mentioning

confidence: 88%

Section: Methodsmentioning

confidence: 99%

Section: Sspb C Terminus Binds a Hydrophobic Patch On The Surface Of mentioning

confidence: 99%

See 2 more Smart Citations

Specificity in substrate and cofactor recognition by the N-terminal domain of the chaperone ClpX

Thibault

Yudin²,

Wong³

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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“…As one of the most popular commercial refractometers, Abbé refractometer could reach 10 −4 RIU by using the total internal reflection phenomenon. The wave optics based methods exploit the wave nature of light and mainly measure the RI by diffraction, 6 forward/backward scattering 7,8 and interference ͑e.g., Fabry-Pérot, [9][10][11] Mach-Zehnder, 12,13 double slits, 14 Michelson, 15 low coherence, 16 and fiber Bragg gratings 17,18 ͒. These methods improve the sensitivity to 10 −4 -10 −6 RIU since the wavelength acts naturally as the absolute reference of length.…”

Section: Introductionmentioning

confidence: 99%

Optofluidic refractometer using resonant optical tunneling effect

et al. 2010

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This paper presents the design and analysis of a liquid refractive index sensor that utilizes a unique physical mechanism of resonant optical tunneling effect ͑ROTE͒. The sensor consists of two hemicylindrical prisms, two air gaps, and a microfluidic channel. All parts can be microfabricated using an optical resin NOA81. Theoretical study shows that this ROTE sensor has extremely sharp transmission peak and achieves a sensitivity of 760 nm/refractive index unit ͑RIU͒ and a detectivity of 85 000 RIU −1 . Although the sensitivity is smaller than that of a typical surface plasmon resonance ͑SPR͒ sensor ͑3200 nm/RIU͒ and is comparable to a 95% reflectivity Fabry-Pérot ͑FP͒ etalon ͑440 nm/RIU͒, the detectivity is 17 000 times larger than that of the SPR sensor and 85 times larger than that of the FP etalon. Such ROTE sensor could potentially achieve an ultrahigh sensitivity of 10 −9 RIU, two orders higher than the best results of current methods.

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Dual Polarization Interferometry: A Real‐Time Optical Technique for Measuring (Bio)molecular Orientation, Structure and Function at the Solid/Liquid Interface

Cross

Freeman²,

Swann³

2007

Handbook of Biosensors and Biochips

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The measurement of proteins, their structure, and function is a crucial step in the characterization, understanding, and utilization of many biological processes. Highly sophisticated structural and functional measurement techniques have been developed over the last 40 years as separate techniques. X‐ray crystallography, nuclear magnetic resonance (NMR) and neutron reflectivity have provided structural measurements, while techniques such as surface plasmon resonance (SPR) or microcalorimetry have provided functional data. Dual polarization interferometry (DPI) is a bench‐top surface analytical technique capable of providing real‐time measurements of molecular (multi)layer dimensions. This enables both structural and functional aspects of biomolecular layers to be determined. Thus molecular immobilization, orientation, assembly, interactions, and stability can be probed, with applications, for example, in biomolecular interactions, drug discovery, sensor surface design, biofouling, and biocompatibility. While generally applicable to a wide range of physicochemical measurement, this chapter gives a few examples of biological applications, highlighting the complementarities of the structural and functional data, rather than mass based response alone, for which there are many other examples.

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A new quantitative optical biosensor for protein characterisation

Cited by 206 publications

References 15 publications

Specificity in substrate and cofactor recognition by the N-terminal domain of the chaperone ClpX

Specificity in substrate and cofactor recognition by the N-terminal domain of the chaperone ClpX

Optofluidic refractometer using resonant optical tunneling effect

Dual Polarization Interferometry: A Real‐Time Optical Technique for Measuring (Bio)molecular Orientation, Structure and Function at the Solid/Liquid Interface

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