Such as DSC, that require the preservation of native protein forms. ![]() The protein concentration (e.g., fractionation), when downstream applications include techniques, Should be taken into account when concentrating dilute samples or employing techniques that lower Protein content, resulted in affected thermogram shapes suggesting changes in protein stability. Structure of proteins present in the solution.Ĭonclusion: Dilution of samples below 0.1 mg/mL, as well as concentration of samples with low We also found a relationship betweenĬhanges in thermograms and low protein concentration, indicating that diluting biospecimens toĬoncentrations below 0.1 mg/mL can perturb the intermolecular environment and affect the That sample processing affects the structure or intermolecular interactions of component proteinsĬontributing to altered thermal stability detectable by DSC. Results: Our studies indicate that both methods can affect protein stability assessed by DSC and,Įven after optimization of several parameters, the obtained DSC profile (thermogram) suggested Of establishing a protocol for DSC analysis of low concentration biospecimens. Methods of sample concentration characterized by a low risk of protein denaturation, with the goal Methods: We evaluated centrifugal concentration and stirred cell ultrafiltration, two common ![]() However, for some techniques, like differential scanning calorimetry (DSC) thatĬharacterizes thermally-induced unfolding of biomolecules, sample processing must not affect This problem, sample processing methods are employed to increase the protein concentration inĪnalyzed samples. Saliva) can be challenging for downstream analysis methods with limited sensitivity. Background: The analysis of biofluid samples with low protein content (e.g., urine or
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