The TolA-recognition Site of Colicin N. ITC, SPR and Stopped-flow Fluorescence Define a Crucial 27-residue Segment

Gökçe, İ̇sa; Raggett, Elaine M.; Hong, Qi; Virden, Richard; Cooper, Alan; Lakey, Jeremy H.

doi:10.1006/jmbi.2000.4232

Cited by 40 publications

(53 citation statements)

References 38 publications

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“…1). Two mutants (S58C and S61C) were chosen at sites in the middle of the binding box known not to affect the binding affinity (13). One mutant (N53C) was set just before the residues critical for the binding, and two mutants (N70C and N71C) were placed just after the binding box.…”

Section: Resultsmentioning

confidence: 99%

“…4). The assumption that each tryptophan is an equal donor of energy could introduce additional uncertainty but Gokce et al (13) showed that their quantum yields are similar. Specific FRET distance measurements are only valid if the donor-acceptor distance is unchanged during the lifetime of the excited state.…”

Section: Discussionmentioning

confidence: 99%

“…Protein samples were allowed to equilibrate at 25°C prior to use and centrifuged to pellet particulate material if necessary. The fluorescence versus time data were analyzed using SX.17MV software version 4.22 exactly as described (13). Concentration of the T-domain mutants was kept at 0.1 M, while TolA-II,III was at least at 10-fold higher concentrations.…”

Section: Stopped-flow Measurements-anmentioning

confidence: 99%

“…SPR Measurements-SPR measurements of T-domain binding to TolA were performed on a BIAcore system as described previously (13). TolA-II,III was immobilized on a CM5 chip.…”

Section: Stopped-flow Measurements-anmentioning

confidence: 99%

“…Exposed to the solvent in the soluble form, they are buried after binding to TolA-III causing an increase and blue-shift of their fluorescence (12). Both are needed for binding and contribute equally to the observed fluorescence change (13). Circular dichroism (CD) and fluorescence studies indicate that the T-domain is unstructured (12), in accord with the x-ray crystallographic structure analysis of colicin N (14) that failed to detect electron density for residues 1-90 of the T-domain, indicating that it is disordered in the crystal.…”

mentioning

confidence: 99%

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Concerted Folding and Binding of a Flexible Colicin Domain to Its Periplasmic Receptor TolA

Anderluh

Hong

Boetzel

et al. 2003

Journal of Biological Chemistry

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Stopped-flow Measurements-anmentioning

confidence: 99%

“…SPR Measurements-SPR measurements of T-domain binding to TolA were performed on a BIAcore system as described previously (13). TolA-II,III was immobilized on a CM5 chip.…”

Section: Stopped-flow Measurements-anmentioning

confidence: 99%

mentioning

confidence: 99%

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Concerted Folding and Binding of a Flexible Colicin Domain to Its Periplasmic Receptor TolA

Anderluh

Hong

Boetzel

et al. 2003

Journal of Biological Chemistry

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High‐Affinity Chelator Thiols for Switchable and Oriented Immobilization of Histidine‐Tagged Proteins: A Generic Platform for Protein Chip Technologies

Tinazli

Tang

Valiokas

et al. 2005

Chemistry A European J

152

149

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Protein micro-/nanoarrays are becoming increasingly important in systematic approaches for the exploration of protein-protein interactions and dynamic protein networks, so there is a high demand for specific, generic, stable, uniform, and locally addressable protein immobilization on solid supports. Here we present multivalent metal-chelating thiols that are suitable for stable binding of histidine-tagged proteins on biocompatible self-assembled monolayers (SAMs). The architectures and physicochemical properties of these SAMs have been probed by various surface-sensitive techniques such as contact angle goniometry, ellipsometry, and infrared reflection-absorption spectroscopy. The specific molecular organization of proteins and protein complexes was demonstrated by surface plasmon resonance, confocal laser scanning, and atomic force microscopy. In contrast to the mono-NTA/His6 tag interaction, which has major drawbacks because of its low affinity and fast dissociation, drastically improved stability of protein binding by these multivalent chelator surfaces was observed. The immobilized histidine-tagged proteins are uniformly oriented and retain their function. At the same time, proteins can be removed from the chip surface under mild conditions (switchability). This new platform for switchable and oriented immobilization should assist proteome-wide wide analyses of protein-protein interactions as well as structural and single-molecule studies.

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Survey of the year 2000 commercial optical biosensor literature

Rich

Myszka

2001

J of Molecular Recognition

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We have compiled a comprehensive list of the articles published in the year 2000 that describe work employing commercial optical biosensors. Selected reviews of interest for the general biosensor user are highlighted. Emerging applications in areas of drug discovery, clinical support, food and environment monitoring, and cell membrane biology are emphasized. In addition, the experimental design and data processing steps necessary to achieve high-quality biosensor data are described and examples of well-performed kinetic analysis are provided.

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The TolA-recognition Site of Colicin N. ITC, SPR and Stopped-flow Fluorescence Define a Crucial 27-residue Segment

Cited by 40 publications

References 38 publications

Concerted Folding and Binding of a Flexible Colicin Domain to Its Periplasmic Receptor TolA

Concerted Folding and Binding of a Flexible Colicin Domain to Its Periplasmic Receptor TolA

High‐Affinity Chelator Thiols for Switchable and Oriented Immobilization of Histidine‐Tagged Proteins: A Generic Platform for Protein Chip Technologies

Survey of the year 2000 commercial optical biosensor literature

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