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To test the behavior of these proteins in semispecifically oriented layers, we covalently modified lysine residues with biotin or sulfhydryl functions, and attached the conjugates to plastic surfaces derivatized with streptavidin or maleimide, respectively.
The study of the behavior of these proteins provide information about the function of chromosomes, since part of the control of the genetic information encoded by DNA depends on interactions with proteins.
Furthermore, we demonstrate that the highly acidic TRs present within the ehrlichial TRPs are responsible for the anomalous electrophoretic behavior of these proteins and not glycosylation.
The interaction of Tim with mitotic entry kinases provoked us to examine the effect of siTim depletion on the cell cycle behavior of these proteins.
Therefore, with the exception of flotillin-1, the behavior of these proteins paralleled that of the total late endosomal protein population depicted in Fig. 1E.
The unusual behavior of these proteins can be explained by an interaction of the membrane with the distinct peptide structure; the charged amino acids in these membrane-inserting cationic peptides have to be evaluated in the overall context and their specific position in the entire peptide [20].
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The upper right and lower left panels of Figures 2 to 5 represent the reversal behavior of these protein coatings.
DNase pretreatment showed minor alterations in the sedimentation behavior of the proteins but these were within the margins of sample variability (Figure 2B).
Based on the behavior of these two proteins, one possibility is that late rRNA processing proteins already interact in PNBs.
We tagged the constructs with EGFP at their carboxyl termini so that we can easily follow the behavior of the proteins synthesized from these constructs.
That is, compared to the behavior of these three proteins in reactions containing untreated intact chloroplasts (refer to Figure 3b, lanes 2 and 3), their binding and integration into trypsin-pretreated chloroplasts was substantially reduced, although to a much lesser extent for myc-Toc34 (Figure 7a).
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