Quantifying CBM–Carbohydrate Interactions Using Microscale Thermophoresis
Quantifying CBM–Carbohydrate Interactions Using Microscale Thermophoresis
MicroScale Thermophoresis (MST) is an emerging technology for studying a broad range of biomolecular interactions with high sensitivity. The affinity constant can be obtained for a wide range of molecules within minutes based on reactions in microliters. Here, we describe the application of MST in quantifying two CBM-carbohydrate interactions, a CBM3a toward cellulose nanocrystals and a CBM4 against xylohexaose.
[SDV.BIO]Life Sciences [q-bio]/Biotechnology, binding studies, [SPI.GPROC] Engineering Sciences [physics]/Chemical and Process Engineering, [SDV]Life Sciences [q-bio], Carbohydrates, fluorescence quenching, Fluorescent label, Chemistry Techniques, Analytical, [SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering, Cellulose, Clostridium, Microscale thermophoresis (MST), Microscale thermophoresis (MST) Binding studies Fluorescence quenching Fluorescent label K d (dissociation constant), Temperature, Proteins, fluorescent label, microscale thermophoresis, [SDV.BIO] Life Sciences [q-bio]/Biotechnology, Binding studies, Fluorescence quenching, [SDV] Life Sciences [q-bio], Carbohydrate Metabolism, K d (dissociation constant), Protein Binding
[SDV.BIO]Life Sciences [q-bio]/Biotechnology, binding studies, [SPI.GPROC] Engineering Sciences [physics]/Chemical and Process Engineering, [SDV]Life Sciences [q-bio], Carbohydrates, fluorescence quenching, Fluorescent label, Chemistry Techniques, Analytical, [SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering, Cellulose, Clostridium, Microscale thermophoresis (MST), Microscale thermophoresis (MST) Binding studies Fluorescence quenching Fluorescent label K d (dissociation constant), Temperature, Proteins, fluorescent label, microscale thermophoresis, [SDV.BIO] Life Sciences [q-bio]/Biotechnology, Binding studies, Fluorescence quenching, [SDV] Life Sciences [q-bio], Carbohydrate Metabolism, K d (dissociation constant), Protein Binding
selected citations These citations are derived from selected sources.This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).5 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Top 10% influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Average impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Average
Citations provided by BIP!Popularity provided by BIP!