Preparation methods have a large influence on the folding and oligomerization behaviour of proteins in solution. In an experiment carried out by Anton Paar, bovine serum albumin (BSA) dissolved in deionized water (BSA-H2O) was compared to BSA re-suspended in the isotonic buffer PBS (BSA-PBS). Particle size results suggested that BSA-H20 had suffered denaturation and/or aggregation, while BSA-PBS primarily consisted in native BSA dimers. Molecular mass measurements performed on BSA-H20 returned erroneous results due to the multimodal nature of the sample, while those performed on BSA-PBS displayed the expected molecular mass of dimeric BSA.
Click on the link above to download this report and see the full details of this experiment and its interesting findings.
Invinity to build 20MWh flow battery in UK
A surprising comment for someone who (I think you´ve said in the past) worked in the industry. National Grid have a variety of reserve service schemes...