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Our goal was to engineer two different TetR chain variants, A and B, that no longer interact as AA or BB homodimers but selectively recombine to form heterodimers.
To determine the role of the alpha-hemoglobin stabilizing protein (AHSP) in the clinical expression of α-hemoglobin (α-Hb) variants described as unstable, ten α chain variants have been studied with their chaperone.
Overall these figures depict that as acyl chain length increases it leads to a decrease of the observed the Kd, suggesting that longer chain AHLs have a higher membrane affinity than the shorter chain variants.
TPP thiols for the longer chain variants were produced from the corresponding bromoalkene [22] (Fig. 2B).
These α-globin chain variants have most likely occurred via recurrent mutations, gene conversion events, or both.
The hematological indices of the subjects carrying these α-globin chain variants are provided in Tables 2 and 3.
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We determined the solution structure of a single chain variant of NpuDnaE intein by NMR spectroscopy.
The sequence described here is the heavy chain variant, containing the feroxidase motif.
A recent meta-analysis demonstrated that an IL4R (IL-4 receptor alpha chain) variant modestly increases risk for atopic asthma [32].
There is additionally a second clathrin heavy chain variant, CHC22, which is predominantly expressed in muscle and is highly similar in sequence to the ubiquitous CHC17 form introduced into the DKO-R cell-line.
One of the most extensively studied targets is the interleukin-13 receptor alpha chain variant 2 (IL13R α2).
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