Search results
Results from the WOW.Com Content Network
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.
Thermostable proteins are often more useful than their non-thermostable counterparts, e.g., DNA polymerase in the polymerase chain reaction, [7] so protein engineering often includes adding mutations to increase thermal stability. Protein crystallization is more successful for proteins with a higher melting point [8] and adding buffer ...
These interactions include salt bridges and hydrogen bonds. Salt bridges are unaffected by high temperatures, therefore, are necessary for protein and enzyme stability. A third force used to increase thermostability in proteins and enzymes is the presence of disulfide bonds. They present covalent cross-linkages between the polypeptide chains.
Cycloheximide chases are also valuable for assessing how different mutations affect the stability of a protein. Experiments have been conducted in yeast and mammalian cells to determine the critical residues required for protein stability and how disease-associated mutations may be affecting protein half-lives within the cell.
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.
Binding of a drug to a protein often leads to ligand-induced stabilization of the protein (1), which can be measured by comparing the amount of non-denatured protein remaining in a drug-treated sample to an untreated control. The change in protein stability can be visualized as a rightward shift in its stability curve (2).
The importance of crowding in protein folding is of particular interest in biophysics. Here, the crowding effect can accelerate the folding process, since a compact folded protein will occupy less volume than an unfolded protein chain. [14] However, crowding can reduce the yield of correctly folded protein by increasing protein aggregation.
In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]