TY - JOUR
T1 - Surface Plasmon Resonance Analysis for Quantifying Protein-Carbohydrate Interactions
AU - Møller, Marie Sofie
AU - Cockburn, Darrell W.
AU - Wilkens, Casper
N1 - Publisher Copyright:
© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
PY - 2023
Y1 - 2023
N2 - During the past two decades, surface plasmon resonance (SPR) analysis has emerged as an important tool for studying protein-carbohydrate interactions, with several commercial instruments available. Binding affinities in the nM to mM range can be determined; however, there are pitfalls that require careful experimental design to avoid. Here we give an overview of each step in the SPR analysis from immobilization to data analysis, providing key points of consideration that will allow practitioners to achieve reliable and reproducible results.
AB - During the past two decades, surface plasmon resonance (SPR) analysis has emerged as an important tool for studying protein-carbohydrate interactions, with several commercial instruments available. Binding affinities in the nM to mM range can be determined; however, there are pitfalls that require careful experimental design to avoid. Here we give an overview of each step in the SPR analysis from immobilization to data analysis, providing key points of consideration that will allow practitioners to achieve reliable and reproducible results.
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U2 - 10.1007/978-1-0716-3151-5_10
DO - 10.1007/978-1-0716-3151-5_10
M3 - Article
C2 - 37149528
AN - SCOPUS:85157977779
SN - 1064-3745
VL - 2657
SP - 141
EP - 150
JO - Methods in molecular biology (Clifton, N.J.)
JF - Methods in molecular biology (Clifton, N.J.)
ER -