Cooperative hydrogen bond interactions in the streptavidin-biotin system
نویسندگان
چکیده
منابع مشابه
Reconsideration of Dynamic Force Spectroscopy Analysis of Streptavidin-Biotin Interactions
To understand and design molecular functions on the basis of molecular recognition processes, the microscopic probing of the energy landscapes of individual interactions in a molecular complex and their dependence on the surrounding conditions is of great importance. Dynamic force spectroscopy (DFS) is a technique that enables us to study the interaction between molecules at the single-molecule...
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Force spectroscopy measurements of the rupture of the molecular bond between biotin and streptavidin often results in a wide distribution of rupture forces. We attribute the long tail of high rupture forces to the nearly simultaneous rupture of more than one molecular bond. To decrease the number of possible bonds, we employed hydrophilic polymeric tethers to attach biotin molecules to the atom...
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Although the generation of hybrid cells by cell fusion plays a significant role in biotechnology and biomedicine, the low cell-fusion rates and the limitation of large-scale cell fusion for clinical applications of the two widely used approaches, polyethylene-glycol (PEG)-mediated cell fusion and electrofusion, hinder the application of this critical technology in certain key areas, including c...
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In this work the properties of a biotin-streptavidin BioFET have been studied numerically with homogenized boundary interface conditions as the link between the oxide of the FET and the analyte which contains the bio-sample. The biotin-streptavidin reaction pair is used in purification and detection of various biomolecules; the strong streptavidin-biotin bond can also be used to attach biomolec...
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(+)-Epi-biotin differs from (+)-biotin in the configuration of the chiral center at atom C2. This could lead to a difference in the mode of binding of (+)-epi-biotin to streptavidin, a natural protein receptor for (+)-biotin. Diffraction data were collected to a maximum of 0.85 Angstrom resolution for structural analysis of the complex of streptavidin with a sample of (+)-epi-biotin and refinem...
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ژورنال
عنوان ژورنال: Protein Science
سال: 2006
ISSN: 0961-8368,1469-896X
DOI: 10.1110/ps.051970306