The ratio of absorbance at 260 nm vs 280 nm is commonly used to assess DNA contamination of protein solutions, since proteins ( in particular, the aromatic amino acids ) absorb light at 280 nm.
22.
Is there a rule of thumb for how concentrated this protein solution can be ? ( I know that if the solution is too concentrated, it causes problems ) ike9898 17 : 08, 11 April 2006 ( UTC)
23.
Because of its ability to disrupt the structure of proteins, it was used in the analysis of proteins, for instance, to ensure that a protein solution contains monomeric protein molecules, instead of disulfide linked dimers or higher order oligomers.
24.
In 1851, German physiologist Otto Funke published a series of articles in which he described growing hemoglobin crystals by successively diluting red blood cells with a solvent such as pure water, alcohol or ether, followed by slow evaporation of the solvent from the resulting protein solution.
25.
To create a protein-stabilized foam, it usually involves bubbling, whipping or shaking a protein solution and its foaming properties refers to its capacity to form a thin tenacious film at the gas-liquid interface for large amounts of gas bubbles to become incorporated and stabilized.
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