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Figure 5 | BMC Biochemistry

Figure 5

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

Figure 5

A synthetic peptide corresponding to the N-terminal domain of atTic20 has characteristics of an intrinsically disordered protein. (A) Temperature-dependent far-UV CD spectra of N-terminal peptide of atTic20. (B) pH-dependent far-UV CD spectra of N-terminal peptide of atTic20. (C) Far-UV CD spectra of N-terminal peptide of atTic20 in the absence and presence of 10% and 50% TFE at 25°C. Peptide content was kept at a concentration of 40 μM in Tris buffer for all measurements. The peptide gained modest amounts of structure with increasing temperature, pH, and TFE concentration, which is consistent with the domain being intrinsically disordered.

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BMC Biochemistry

ISSN: 1471-2091

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