GiftBox.com is a official representative of the following brands:Â .Molecular properties of cyclophilin A.
As more protein structures have been determined by X-ray crystallography and three-dimensional nuclear magnetic resonance spectroscopy, the methods of studying the conformational properties of proteins have also improved. In this study, we compared the conformational properties of peptide backbone protons in the cyclophilin A from a number of different sources. Our finding of conformational differences for certain well-defined protons may be due to the fact that individual cyclophilin A molecules may exist in solution with different amounts of energy depending on their quaternary structure and how they interact with their ligand. of the energy E, entailing thus the normalizing factor $\frac{1}{2}\left( 1-\cos k_{z}\right)$. For the special case $V_{0}=0$, the magnetic field is always divergent for the symmetric case where $\left\vert \xi \right\vert =N/2$ and $\kappa=1$. We can thus define this divergence by the following relation:

$$\left\langle B_{z}(0,0)\right\rangle _{0}=\frac{1}{2}N\left( \xi \right) \frac{1}{1-\cos\left( \frac{\pi N}{2}\right) }\text{,} \label{V_0_nil}$$

and then evaluate it in the limit $N\rightarrow\infty$ in order to find

$$\left\langle B_{z}(0,0)\right\rangle _{0}=\frac{1}{2}\text{.} \label{V_0_min}$$

A similar divergence in the magnetic field can be found for the case $\left\vert \xi\right\vert eq N/2$ and $\kappa=1$, yielding:

\left\langle B_{z}(\xi)\right\rangle _{0}=\frac{1}{2}\left[ \left(
N

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