That's all there is to it. If we plot this, the x-axis intercept will be the Bound(max).
We have to transform the data so that it makes sense. The raw data given in the question is "relative fluorescence" and "protein concentration." ...
Solution Summary
The solution provides the required sacatchard plot of the data in an attached excel sheet along with an explanation of what this represents and how to determine the maximum binding constant from the graph just formed.
Consider a small, natively disordered protein that exists in equilibrium with a highly ordered (folded) protein. At 37°C, the ratio of the disordered protein to ordered is 100 to 1. First, write an equilibrium expression (Keq) that describes this situation and calculate the corresponding Keq and free energy. Second, imagine
Expand the given sketch of a proof into a reasonably complete proof.
It is suggested that the following proof be used:
Maximum Modulus Principle: Let U be a non-empty open subset of the complex numbers C, let D(z0,r)={z є C: |z-z0| ≤ r} be a closed disk (with center z0 and radius r >0) that is entirely contained in U, le
(See attached file for full problem description)
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For problems 6-8, assume standard conditions of pH 7 and 25C, unless otherwise stated, and assume equilibrium constants in which any [H+] and [H2O] terms have been incorporated into theconstant, i.e., you don't have to use [H+] in any of the calculations.
6. Th
In this experiment we used electrophoresis to study thebinding interactions that occure between serum albumin and two synthetic dyes. The dyes were Bromophenol Blue and Ponceau S. The basis for this procedure was the observation that the free dyes not bound to albumin migrate faster than albumin or dyes bound to albumin.
I
You are a scientist working on a large protein (500 amino acids long) you have genetically engineered theprotein in in such a way as to replace a single hydrophobic amino acid with a negatively charged amino acid. How might this substitution alter the primary and the tertiary structure of theprotein? How will the nutritional
The galactose represser protein from E. coli has a pI of about 5.9. While purification protocols were being designed, it was found to bind to a Mono-S column at pH values of 7 and below. (Mono-S columns have S-type sulfonic acid groups attached to the resin and are strong cation exchangers.)
What is unusual about this observ
See attached a pdf file.
You can find more Mobius transformation information from John Conway - Functions of One Complex Variable I or Serge Lang - Complex Analysis or other Complex Analysis books.
Problem of Schwarz's Lemma
1. Suppose f: D → ¢ satisfies Re f(z) ≥ 0 for all z in D and suppose that f is analytic and
What is complex data binding? What advantages can this capability lend to a multiple-table database application? Present an example of a situation where complexbinding would be appropriate in an application and discuss why this approach is needed in this scenario.
