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Region Hovedstaden - en del af Københavns Universitetshospital
Udgivet

Determination of Binding Kinetics of Intrinsically Disordered Proteins by Surface Plasmon Resonance

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  1. Analysis of Mass Cytometry Data

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  2. Assessment of Peptidylarginine Deiminase Activity by ELISA Using Human Fibrinogen as Substrate

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  3. Full-Length Open Reading Frame Amplification of Hepatitis C Virus

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  4. In Vitro Neutralization Assay Using Cultured Hepatitis C Virus

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  5. Noninvasive Antenatal Screening for Fetal RHD in RhD Negative Women to Guide Targeted Anti-D Prophylaxis

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  1. Chylomicronemia from GPIHBP1 autoantibodies

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  2. Disorder in a two-domain neuronal Ca2+-binding protein regulates domain stability and dynamics using ligand mimicry

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  3. Chylomicronemia From GPIHBP1 Autoantibodies Successfully Treated With Rituximab: A Case Report

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  4. The structural basis for monoclonal antibody 5D2 binding to the tryptophan-rich loop of lipoprotein lipase

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Vis graf over relationer

Surface plasmon resonance (SPR) is an important and convenient method for measuring kinetic rate constants of given molecular interactions, equilibrium binding constants at steady state, or determinations of binding stoichiometry. In its traditional setup, SPR requires that one binding partner is tightly immobilized on the surface of a sensor chip either by direct chemical coupling to the surface-coated carboxymethylated dextran matrix or by non-covalent capture to a high-affinity binding partner that is covalently linked to the surface. The latter design of the sensor surface is highly advantageous compared to the direct chemical coupling as this setup ensures a homogeneous and specific orientation of the immobilized binding partner. This chapter provides guidelines for the design of capturing systems that generally provide high-end kinetic data suitable for determination of binding rate constants. This principle will be illustrated by the binding of synthetic peptides derived from an intrinsically disordered region of the endothelial glycosylphosphatidylinositol-anchored high-density lipoprotein binding protein 1 (GPIHBP1) to captured monoclonal antibodies.

OriginalsprogEngelsk
TidsskriftMethods in Molecular Biology
Vol/bind2141
Sider (fra-til)611-627
Antal sider17
ISSN1064-3745
DOI
StatusUdgivet - 2020

ID: 60627027