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A ten-fold serial dilution could be 1 M, 0.1 M, 0.01 M, 0.001 M ... Serial dilutions are used to accurately create highly diluted solutions as well as solutions for experiments resulting in concentration curves with a logarithmic scale.
For example, on a plot axis showing log 2 fold changes, an 8-fold increase will be displayed at an axis value of 3 (since 2 3 = 8). However, there is no mathematical reason to only use logarithm to base 2, and due to many discrepancies in describing the log 2 fold changes in gene/protein expression, a new term "loget" has been proposed. [10]
The postulate amounts to saying that, at the environmental conditions (temperature, solvent concentration and composition, etc.) at which folding occurs, the native structure is a unique, stable and kinetically accessible minimum of the free energy. In other words, there are three conditions for formation of a unique protein structure:
In the less extensive technique of equilibrium unfolding, the fractions of folded and unfolded molecules (denoted as and , respectively) are measured as the solution conditions are gradually changed from those favoring the native state to those favoring the unfolded state, e.g., by adding a denaturant such as guanidinium hydrochloride or urea.
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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 summary, in order to find a standard curve, one must use varying concentrations of BSA (Bovine Serum Albumin) [2] in order to create a standard curve with concentration plotted on the x-axis and absorbance plotted on the y-axis. Only a narrow concentration of BSA is used (2-10 ug/mL) in order to create an accurate standard curve. [23]