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Open AccessJournal ArticleDOI

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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Journal ArticleDOI

Biophysical characterization of laforin–carbohydrate interaction

TL;DR: The work in the present study complements the structural characterization of la forin and sheds light on the molecular mechanism of laforin-glycan interaction, which is a pivotal requisite to understand the physiological and pathological roles of Laforin.
Journal ArticleDOI

Functional characterisation of G protein-coupled receptors.

TL;DR: This review focuses on G protein-coupled receptors (GPCRs), examining techniques that can be applied to both receptors in membranes and after solubilisation, and a variety of experimental techniques available to incorporate suitable donors and acceptors within the receptor.
Journal ArticleDOI

19F NMR as a Tool for Monitoring Individual Differentially Labeled Proteins in Complex Mixtures

TL;DR: This study proposes differential labeling of proteins by covalent attachment of 19F groups with distinct chemical shifts, giving each protein a unique spectral signature which can be monitored by 19F NMR without signal overlap, even in complex mixtures, and without any interfering signals from the buffer or other unlabeled components.
Journal ArticleDOI

Studying epigenetic interactions using MicroScale Thermophoresis (MST)

TL;DR: The MicroScale Thermophoresis (MST) is a rapid and precise method to characterize epigenetic interactions in solution at microliter scale, requiring low concentrations of the potential interactors.
Book ChapterDOI

Biophysical Analysis of Sec-Mediated Protein Translocation in Nanodiscs

TL;DR: Cryo-electron microscopy of nanodisc-reconstituted SecYEG and YidC in complex with ribosomes visualized intermediates on membrane protein insertion and demonstrated structural dynamics of insertases, and suggestednanodiscs as a powerful platform for further studies, including high-resolution structural analysis.
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.
Journal ArticleDOI

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.
Journal ArticleDOI

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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