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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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Notch Activation by Shootin1 Opposing Activities on 2 Ubiquitin Ligases.

TL;DR: It is identified that Shootin1 exhibits the surprising propensity of activating the Notch pathway either by interacting with LNX1/2 and promoting poly-ubiquitination of Numb or by complexing with Itch and impairing poly-UBiquitinations of NICD.
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Biophysical Characterisation and Quantification of Nucleic Acid-Protein Interactions: EMSA, MST and SPR.

TL;DR: Three techniques that are commonly used to quantify and characterize DNA-protein and RNA-protein interactions are presented and their main advantages and limitations are discussed.
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Non-full-length Water-Soluble CXCR4QTY and CCR5QTY Chemokine Receptors: Implication for Overlooked Truncated but Functional Membrane Receptors.

TL;DR: Insight is provided into essential structural components for CCR5 and CXCR4 functionality, while raising the possibility that non-full-length receptors may be resulted from alternative splicing and that pseudo-genes in genomes may be present and functional in living organisms.
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Tampering with Cell Division by Using Small‐Molecule Inhibitors of CDK–CKS Protein Interactions

TL;DR: Two small‐molecule inhibitors ofCDK–CKS interactions are discovered that should help decipher the complex contributions of CDK-CKS complexes in the regulation of cell division and might present an interesting therapeutic potential.
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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