Monitoring protein aggregation during thermal unfolding in circular dichroism experiments

Thermal unfolding monitored by spectroscopy or calorimetry is widely used to determine protein stability. Equilibrium thermodynamic analysis of such unfolding is often hampered by its irreversibility, which usually results from aggregation of thermally denatured protein. In addition, heat‐induced pr...

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Veröffentlicht in:	Protein science 2006-03, Vol.15 (3), p.635-639
Hauptverfasser:	Benjwal, Sangeeta, Verma, Shikha, Röhm, Klaus‐Heinrich, Gursky, Olga
Format:	Artikel
Sprache:	eng
Schlagworte:	aggregation amyloid apoC‐1, apolipoprotein C‐1 Asparaginase - chemistry asparaginase‐2 CD, circular dichroism Circular Dichroism - methods circular dichroism spectroscopy conformational changes DMPC, dimyristoyl phosphatidylcholine DSC, differential scanning calorimetry EcA2, asparaginase isoenzyme 2 from E. coli enzymes For the Record high‐density lipoprotein hydrodynamics irreversible protein unfolding Light light scattering Lipoproteins - chemistry Protein Conformation Protein Denaturation Protein Folding protein structure/folding Proteins - chemistry Scattering, Radiation Spectrophotometry, Ultraviolet stability and mutagenesis Temperature thermodynamics turbidity
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