ArticleBio-protocol2017
MicroScale Thermophoresis as a Tool to Study Protein-peptide Interactions in the Context of Large Eukaryotic Protein Complexes.
Article in Bio-protocol, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 19 citations in OpenAlex.
- PUF family RNA-binding proteins Puf1 and Puf2 promote transcript degradation in Toxoplasma gondii.The Journal of biological chemistry · 2026Article
- Measuring Interactions Between Proteins and Small Molecules or Nucleic Acids.Current protocols · 2024Review
- Virtual Screening of Peptide Libraries: The Search for Peptide-Based Therapeutics Using Computational Tools.International journal of molecular sciences · 2024Review
- Binding of human ACE2 and RBD of Omicron enhanced by unique interaction patterns among SARS-CoV-2 variants of concern.Journal of computational chemistry · 2023Article
- The Phytophthora sojae nuclear effector PsAvh110 targets a host transcriptional complex to modulate plant immunity.The Plant cell · 2023Article
- Binding Affinity Measurements Between DNA Aptamers and their Virus Targets Using ELONA and MST.Bio-protocol · 2022Article
- Microscale Thermophoresis as a Tool to Study Protein Interactions and Their Implication in Human Diseases.International journal of molecular sciences · 2022Review
- Binding of Human ACE2 and RBD of Omicron Enhanced by Unique Interaction Patterns Among SARS-CoV-2 Variants of Concern.bioRxiv : the preprint server for biology · 2022Article
- Alignment of helicases on single-stranded DNA increases activity.Methods in enzymology · 2022Article
- Differential Interactions between Human ACE2 and Spike RBD of SARS-CoV-2 Variants of Concern.Journal of chemical theory and computation · 2021Article
- MRBLE-pep Measurements Reveal Accurate Binding Affinities for B56, a PP2A Regulatory Subunit.ACS measurement science au · 2021Article
- Differential Interactions Between Human ACE2 and Spike RBD of SARS-CoV-2 Variants of Concern.bioRxiv : the preprint server for biology · 2021Article
- Microscale thermophoresis analysis of the molecular interaction between small nuclear ribonucleoprotein polypeptide G and the RING finger domain of RBBP6 towards anti-cancer drug discovery.American journal of translational research · 2021Article
- Evaluating Iso-Mukaadial Acetate and Ursolic Acid Acetate asBiomolecules · 2019Article
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein-peptide interactions are part of many physiological processes, for example, epigenetics where peptide regions of histone complexes are crucial for regulation of chromatin structure. Short peptides are often also used as alternatives to small molecule drugs to target protein complexes. Studying the interactions between proteins and peptides is thus an important task in systems biology, cell biology, biochemistry, and drug design. However, this task is often hampered by the drawbacks of classical biophysical methods for analysis of molecular interactions like surface plasmon resonance (SPR) or isothermal titration calorimetry (ITC), which require immobilization of the interaction partners or very high sample concentrations. MicroScale Thermophoresis (MST) is an innovative method that offers the possibility to determine the important parameters of a molecular interaction, such as dissociation constant, stoichiometry, and thermodynamics. Moreover, it does so in a rapid and precise manner, with free choice of buffers or biological liquids, no need for sample immobilization, and very low sample consumption. Here we describe two MST assays in detail, which analyze (i) the interactions between certain peptide stretches of the eukaryotic RNA polymerase II and a protein subunit of the eukaryotic transcription elongation complex and (ii) interactions between N-terminal histone tail peptides and epigenetic reader proteins. These experiments show that MST is able to characterize protein-peptide interactions that are triggered by only minor changes in the peptide, for example, only one phosphorylation at a specific serine residue.
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