Three-dimensional structures of avidin and the avidin-biotin complex.

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Three-dimensional structures of avidin and the avidin-biotin complex.

The crystal structures of a deglycosylated form of the egg-white glycoprotein avidin and of its complex with biotin have been determined to 2.6 and 3.0 A, respectively. The structures reveal the amino acid residues critical for stabilization of the tetrameric assembly and for the exceptionally tight binding of biotin. Each monomer is an eight-stranded antiparallel beta-barrel, remarkably simila...

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Unbinding biotin from avidin

Atomic force microscopy of single molecules, steered molecular dynamics and the theory of stochastic processes have established a new field that investigates mechanical functions of proteins, such as ligand–receptor binding/unbinding and elasticity of muscle proteins during stretching. The combination of these methods yields information on the energy landscape that controls mechanical function ...

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Molecular dynamics study of unbinding of the avidin-biotin complex.

We report molecular dynamics simulations that induce, over periods of 40-500 ps, the unbinding of biotin from avidin by means of external harmonic forces with force constants close to those of AFM cantilevers. The applied forces are sufficiently large to reduce the overall binding energy enough to yield unbinding within the measurement time. Our study complements earlier work on biotin-streptav...

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Chicken avidin-related proteins show altered biotin-binding and physico-chemical properties as compared with avidin.

Chicken avidin and bacterial streptavidin are proteins familiar from their use in various (strept)avidin-biotin technological applications. Avidin binds the vitamin biotin with the highest affinity known for non-covalent interactions found in nature. The gene encoding avidin (AVD) has homologues in chicken, named avidin-related genes (AVRs). In the present study we used the AVR genes to produce...

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A Spectrophotometric Assay for Avidin and Biotin Based on Binding of Dyes by Avidin.

The binding of aniohic dyes by serum albumin has been studied by many workers (reviewed by Foster, 1960). The evidence suggests several cationic sites situated in hydrophobic regions of the molecule. For example, the bound dye shows spectral changes that are in accord with its location in a non-polar environment. Since it was suggested (Green, 1963b) that the biotin-binding sites of avidin were...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 1993

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.90.11.5076