Probing Protein Folding with Sequence-Reversed α-Helical Bundles

• Published in: International journal of molecular sciences Vol. 22; no. 4; p. 1955
• Main Authors: Kefala, Aikaterini, Amprazi, Maria, Mylonas, Efstratios, Kotsifaki, Dina, Providaki, Mary, Pozidis, Charalambos, Fotiadou, Melina, Kokkinidis, Michael
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI 16.02.2021
• Subjects: Amino Acid Motifs; Amino Acid Sequence; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Chromatography, Gel; Circular Dichroism; Escherichia coli - genetics; Escherichia coli - metabolism; Models, Molecular; Peptides; Protein Conformation, alpha-Helical; Protein Folding; RNA-Binding Proteins - chemistry; RNA-Binding Proteins - genetics; Scattering, Small Angle; X-Ray Diffraction; coiled-coil proteins; α-helix; polypeptide chain directionality; circular dichroism (CD); protein folding; 4-α-helical bundle; RM6 protein; rop protein; multiangle laser light scattering (MALS); small angle X-ray scattering (SAXS)

Recurrent protein folding motifs include various types of helical bundles formed by α-helices that supercoil around each other. While specific patterns of amino acid residues (heptad repeats) characterize the highly versatile folding motif of four-α-helical bundles, the significance of the polypepti...