Circular dichroism studies on synthetic signal peptides.
Circular dichroism studies on synthetic peptides corresponding to the signal sequences of chicken lysozyme and Escherichia coli proteins, lambda-receptor and lipoprotein, have been carried out in trifluoroethanol. The peptides, (CH3)3-C-O-CO-Thr-Leu-Lys-Lys-Leu-Pro-Leu-Ala-Val-Ala-Val-Ala-Ala-Gly- Val-Met-Thr-Ala- Ala-Met-Ala-OCH3, (CH3)3-C-O-CO-Met-Lys-Ser-Leu-Leu-Ile-Leu-Val-Leu-Cys(benzyl)- Phe-Leu-Pro- Leu-Ala-Ala-Leu-Gly-OH and (CH3)3-C-O-CO-Leu-Val-Leu-Gly-Ala-Val-Ile-Leu-Gly- Thr-Thr-Leu-Leu- Ala-Gly-OCH3, corresponding to the signal sequences of lambda-receptor, lysozyme and the hydrophobic region of lipoprotein, respectively, show two negative bands at approx. 205 and 220 nm, characteristic of an alpha-helical conformation. Secondary structural features are discernible even in the shorter, 12-residue carboxy-terminal fragments of these signal peptides. A comparison of the conformation of the amino-terminal, central and carboxy-terminal fragments of lipoprotein signal sequence indicates that the central octapeptide fragment is more structurally ordered compared to the amino- and carboxy-terminal fragments.
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Nagaraj
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D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D010582:Bacteriophage lambda; D002942:Circular Dichroism; D004926:Escherichia coli; D008074:Lipoproteins; D009113:Muramidase; D011487:Protein Conformation; D021382:Protein Sorting Signals / Q000138:chemical synthesis*; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D008074:Lipoproteins; D021382:Protein Sorting Signals; D009113:Muramidase