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Crystal structure of β-glucosidase from Thermotoga neapolitana (PDB: 5IDI).Thermostable protein, active at 80°C and with unfolding temperature of 101°C. [1]In materials science and molecular biology, thermostability is the ability of a substance to resist irreversible change in its chemical or physical structure, often by resisting decomposition or polymerization, at a high relative ...
Guruprasad K, Reddy BV, Pandit MW (1990). "Correlation between stability of a protein and its dipeptide composition: a novel approach for predicting in vivo stability of a protein from its primary sequence".
Thermodynamic stability of proteins represents the free energy difference between the folded and unfolded protein states. This free energy difference is very sensitive to temperature, hence a change in temperature may result in unfolding or denaturation.
Size exclusion chromatography can be used directly to access protein stability in the presence or absence of ligands. [31] Samples of purified protein are heated in a water bath or thermocycler, cooled, centrifuged to remove aggregated proteins, and run on an analytical HPLC. As the melting temperature is reached and protein precipitates or ...
The resulting crosslinked proteins or protein complexes have been shown to exhibit increased stability towards thermal and chemical stress and a lower tendency towards aggregation. [ 1 ] [ 6 ] So far, the melting temperature of proteins was increased by up to 39°C in a single design step.
Cycloheximide chase assays are an experimental technique used in molecular and cellular biology to measure steady state protein stability. Cycloheximide is a drug that inhibits the elongation step in eukaryotic protein translation, thereby preventing protein synthesis. [1]
It is a most commonly observed contribution to the stability to the entropically unfavorable folded conformation of proteins. Although non-covalent interactions are known to be relatively weak interactions, small stabilizing interactions can add up to make an important contribution to the overall stability of a conformer. [1]
where is the stability of the protein in water and [D] is the denaturant concentration. Thus the analysis of denaturation data with this model requires 7 parameters: Δ G w {\displaystyle \Delta G_{w}} , Δ n {\displaystyle \Delta n} , k , and the slopes and intercepts of the folded and unfolded state baselines.