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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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End-Point Binding Free Energy Calculation with MM/PBSA and MM/GBSA: Strategies and Applications in Drug Design

TL;DR: In this review, methods to adjust the polar solvation energy and to improve the performance of MM/PBSA and MM/GBSA calculations are reviewed and discussed and guidance is provided for practically applying these methods in drug design and related research fields.
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MicroScale Thermophoresis: Interaction analysis and beyond

TL;DR: This review presents recent progress and developments in MST technology and introduces alternative MST applications – such as determination of binding stoichiometries and binding modes, analysis of protein unfolding, thermodynamics and enzyme kinetics, as well as demonstrating the capability of MST to quantify high-affinity interactions with dissociation constants in the low picomolar (pM) range.
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Nanodiscs in Membrane Biochemistry and Biophysics

TL;DR: This review attempted to combine a comprehensive list of various applications of nanodisc technology with systematic analysis of the most attractive features of this system and advantages provided by nanodISCs for structural and mechanistic studies of membrane proteins.
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Assessing the performance of the MM/PBSA and MM/GBSA methods. 6. Capability to predict protein-protein binding free energies and re-rank binding poses generated by protein-protein docking.

TL;DR: The results illustrate that the MM/GBSA rescoring has better capability to distinguish the correct binding structures from the decoys than the ZDOCK scoring and may be a good choice for predicting the binding affinities and identifying correctbinding structures for protein-protein systems.
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Quercetin as an Antiviral Agent Inhibits Influenza A Virus (IAV) Entry

TL;DR: It is indicated that quercetin showing inhibitory activity in the early stage of influenza infection provides a future therapeutic option to develop effective, safe and affordable natural products for the treatment and prophylaxis of IAV infections.
References
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Journal ArticleDOI

Phosphatidylinositol phosphates as co-activators of Ca2+ binding to C2 domains of synaptotagmin 1.

TL;DR: Clear distinctions are revealed in the Ca2+-dependent phospholipid binding modes of the synaptotagmin 1 C2 domains that may underlie their functional asymmetry and suggest that phosphatidylinositol polyphosphates may serve as physiological modulators of Ca2+.
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Phosphatidylinositol 4,5-bisphosphate increases Ca2+ affinity of synaptotagmin-1 by 40-fold

TL;DR: Microscale thermophoresis shows that PIP2 binding to the polybasic patch of synaptotagmin-1 increases the Ca2+ affinity by >40-fold, which shows that this interplay between Ca2+, synaptolipid phosphatidylinositol 4,5-bisphosphate, and PIP1 is crucial for neurotransmitter release.
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Biophysical characterization of the interaction of the beta-lactamase TEM-1 with its protein inhibitor BLIP.

TL;DR: It is shown that simple electrostatic rules can explain the tight interaction of BLIP, expressed heterologousely in E. coli, with TEM-1, and that a limited role for electrostatic forces in guiding this reaction is suggested.
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Binding Hot Spots in the TEM1–BLIP Interface in Light of its Modular Architecture

TL;DR: This study extends to cover the entire interface of TEM1 beta-lactamase and its protein inhibitor BLIP using an improved method for deriving interaction maps based on REDUCE to add hydrogen atoms and then by evaluating the interactions using modifications of the programs PROBE, NCI and PARE.
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Free-Solution, Label-Free Protein-Protein Interactions Characterized by Dynamic Light Scattering

TL;DR: This nondestructive technique enabled determination of stoichiometry of binding, equilibrium dissociation constant, and thermodynamic parameters, as well as the impact of temperature, buffer salinity, and a small-molecule inhibitor.
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