Effects of temperature on the mitochondrial malate dehydrogenase of adult muscle of<i>Toxocara canis</i>

Mansini, E.; Oestreicher, Enrique G.; Ribeiro, Luiz P.

doi:10.3109/13813458909075076

Cited by 2 publications

(1 citation statement)

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“…Currently, interpretation of most DSF experiments assumes that protein unfolding is dominated by thermodynamic contributions, yet the results of extensive CD and DSC studies have suggested that kinetics plays a major role, especially for thermal unfolding 35,36 37 and a model kinetic unfolder (malate dehydrogenase; MDH) 38 were analyzed by DSF at systematically increased heating rates (0.5, 1, 2 and 4 ºC/min; Figure 1a). As expected, we found that the calculated Tma value for lysozyme (69 °C) was largely unaffected by heating rate (∆Tma of only 0.8 °C, calculated between the extreme heating rates of 0.25 and 2 ºC/min; Figure 1b, c).…”

Section: Resultsmentioning

confidence: 99%

Three Essential Resources to Improve Differential Scanning Fluorimetry (DSF) Experiments

Gale-Day

et al. 2020

Preprint

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Differential Scanning Fluorimetry (DSF) is a method that enables rapid determination of a protein's apparent melting temperature (Tma). Owing to its high throughput, DSF has found widespread application in fields ranging from structural biology to chemical screening. Yet DSF has developed two opposing reputations: one as an indispensable laboratory tool to probe protein stability, another as a frustrating platform that often fails. Here, we aim to reconcile these disparate reputations and help users perform more successful DSF experiments with three resources: an updated, interactive theoretical framework, practical tips, and online data analysis. We anticipate that these resources, made available online at DSFworld (https://gestwickilab.shinyapps.io/dsfworld/), will broaden the utility of DSF.Introduction.

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Section: Resultsmentioning

confidence: 99%