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Microscale thermophoresis quantifies biomolecular interactions under previously challenging conditions

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TLDR
Flexibility in assay design qualifies MST for analysis of biomolecular interactions in complex experimental settings, which is demonstrated by addressing typically challenging types of binding events from various fields of life science.
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This article is published in Methods.The article was published on 2013-03-01 and is currently open access. It has received 508 citations till now. The article focuses on the topics: Microscale thermophoresis & Thermophoresis.

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Acquired mutations in BCL2 family proteins conferring resistance to the BH3 mimetic ABT-199 in lymphoma.

TL;DR: The acquisition of mutations in BCL2 family proteins as a novel mechanism of apoptosis resistance in cancer is revealed, providing a basis to preventing their occurrence and to designing drugs able to circumvent the acquired resistance.
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The myosin mesa and the basis of hypercontractility caused by hypertrophic cardiomyopathy mutations.

TL;DR: It is proposed that hypercontractility is due to an increase in the number of myosin heads (S1) that are accessible for force production and that phosphorylation of either S1 or MyBP-C weakens these interactions.
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Pathogen Inhibition by Multivalent Ligand Architectures

TL;DR: The main issues and concerns associated with blocking pathogen at interfaces are highlighted, which are dependent on the nature and properties of both multivalent inhibitors and pathogens, such as viruses and bacteria.
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Rapid and Label-Free Strategy to Isolate Aptamers for Metal Ions

TL;DR: An aptamer discovery method is reported that enables us to generate high-quality structure-switching aptamers (SSAs) that undergo a conformational change upon binding a metal ion target, without the requirement of labels or chemical modifications.
References
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Journal ArticleDOI

Rapid measurement of binding constants and heats of binding using a new titration calorimeter.

TL;DR: A new titration calorimeter is described and results are presented for the binding of cytidine 2'-monophosphate (2'CMP) to the active site of ribonuclease A.
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A gel electrophoresis method for quantifying the binding of proteins to specific DNA regions: application to components of the Escherichia coli lactose operon regulatory system

TL;DR: It is demonstrated that even when pre-formed in the presence of CAP-cAMP, the polymerase-promoter open complex becomes unstable if CAP is then selectively removed, and this gel method is applied to the study of the E. coli lactose operon regulatory system.
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Electrophoretic mobility shift assay (EMSA) for detecting protein-nucleic acid interactions.

TL;DR: The most important factors that determine the stabilities and electrophoretic mobilities of complexes under assay conditions are identified and commonly used variants are discussed.
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Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling.

TL;DR: The results indicate that the Grbl/hSos1 complex couples activated EGF receptor to Ras signalling, and a synthetic 10-amino-acid peptide containing the sequence PPVPPR specifically blocks the interaction.
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