Three-dimensional Structure of the Tetragonal Crystal Form of Egg-white Avidin in its functional Complex with Biotin at 2·7 Å Resolution

Pugliese, Luisa; Coda, Alessandro; Malcovati, Massimo; Bolognesi, Martino

doi:10.1006/jmbi.1993.1321

Cited by 303 publications

(316 citation statements)

References 0 publications

Supporting

Mentioning

292

Contrasting

Order By: Relevance

“…The peak birefringence frequency (f p ), average nanoparticle diameter (d h ), and change in diameter (Δd h ) following each biological binding reaction are summarized in Table 1. The measured nanoparticle diameter increases by 7.8 nm following avidin coating, an increase that is consistent with the addition of a monolayer of avidin, which has a ∼4 nm diameter [18]. Similarly, the diameter increases by 14.2 nm following functionalization with anti-IgG antibodies and by 10.2 nm following incubation with IgG.…”

Section: Resultssupporting

confidence: 67%

Frequency-domain birefringence measurement of biological binding to magnetic nanoparticles

Chan

et al. 2008

Journal of Magnetism and Magnetic Materials

View full text Add to dashboard Cite

Optical detection of the frequency-dependent magnetic relaxation signal is used to monitor the binding of biological molecules to magnetic nanoparticles in a ferrofluid. Biological binding reactions cause changes in the magnetic relaxation signal due to an increase in the average hydrodynamic diameter of the nanoparticles. To allow the relaxation signal to be detected in dilute ferrofluids, measurements are made using a balanced photodetector, resulting in a 25 μV/√Hz noise floor, within 50% of the theoretical limit imposed by photon shot noise. Measurements of a ferrofluid composed of magnetite nanoparticles coated with anti-IgG antibodies show that the average hydrodynamic diameter increases from 115.2 to 125.4 nm after reaction with IgG.

show abstract

Section: Resultssupporting

confidence: 67%

Frequency-domain birefringence measurement of biological binding to magnetic nanoparticles

Chan

et al. 2008

Journal of Magnetism and Magnetic Materials

View full text Add to dashboard Cite

show abstract

“…The comparison of hen egg avidin and streptavidin recently reported by Pugliese et al [9], which showed them to have only trivial structural differences, suggests that the structural similarity reported here for streptavidin should hold for all avidins. Equally, comparisons of known FABP [lo] and lipocalin [5] structures indicates that this relationship is generally true across all of the families.…”

Section: Discussionsupporting

confidence: 66%

Structural relationship of streptavidin to the calycin protein superfamily

Flower

1993

FEBS Letters

View full text Add to dashboard Cite

Streptavidin is a binding protein, from the bacteria Streptomyces av~dznu, with remarkable affinity for the vitamin biotin. The lipocalins and the fatty acid-binding proteins (FABPs), are two other protein families which also act by binding small hydrophobic molecules. Within a similar overall folding pattern (a p-barrel with a repeated +l topology), large parts of the lipocalin, FABP, and streptavidin molecules can be structurally equivalenced. The first structurally conserved region within the three-dimensional alignment, or common core, characteristic of the three groups corresponds to an unusual structural feature (a short 3,,, helix leading into a B-strand, the first of the barrel), conserved in both its conformation and its location within their folds, which also displays characteristic sequence conservation. These similarities of structure and sequence suggest that all three families form part of a larger group: the calycin structural superfamily.

show abstract

“…Previously we reported that avidin, a chicken (Gallus gallus) glycoprotein composed of four glycosylated subunits [12][13][14] , is toxic to seven species of stored-product beetles (Coleoptera) and moths (Lepidoptera) 15 . Avidin and a related protein, streptavidin, produced by the bacterium Streptomyces avidinii, exhibit one of the highest known affinities in nature between a protein and their ligand, biotin (K a = 10 15 M -1 ).…”

Section: Research Articlesmentioning

confidence: 99%