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Figure 1 | BMC Biochemistry

Figure 1

From: Folding and self-association of atTic20 in lipid membranes: implications for understanding protein transport across the inner envelope membrane of chloroplasts

Figure 1

Design of atTic20, its truncated mutant and extramembrane N-terminal peptide. (A) Schematic representation of different forms of atTic20 used in this study. A cDNA encoding pre-atTic20 (including the transit peptide) was used to generate constructs encoding mature atTic20 and atTic20ΔN20, a truncated mutant lacking the 20 amino acid N-terminal domain (NTD), with C-terminal hexahistidine tags (6His). A 21-amino acid peptide corresponding to the NTD was also synthesized (amino acid sequence shown). (B) Results of in silico analyses suggest that atTic20 contains four transmembrane domains and that its N-terminal peptide is disordered. (i) IUPred was used for disorder predictions of atTic20. Transmembrane prediction for atTic20 was based on (ii) hydrophobicity plot and (iii) TMHMM analysis. Refer to the Methods for further detailed method and analysis.

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BMC Biochemistry

ISSN: 1471-2091

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