Expression, purification and crystallization of a protein resulting from the inversion of the amino‐acid sequence of a helical bundle

• Published in: Acta crystallographica. Section F, Structural biology communications Vol. 73; no. 1; pp. 51 - 53
• Main Authors: Kefala, Aikaterini, Kotsifaki, Dina, Providaki, Mary, Amprazi, Maria, Kokkinidis, Michael
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.01.2017; Wiley Subscription Services, Inc
• Subjects: Amino Acid Sequence; Amino acids; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Bundling; Cloning, Molecular; Crystallization; Crystallography; Crystallography, X-Ray; Crystals; E coli; Escherichia coli; Escherichia coli - genetics; Escherichia coli - metabolism; Gene Expression; Helices; heptad repeat; hyperthermophilic protein; Inverse; Inversions; Plasmids - chemistry; Plasmids - metabolism; Protein Conformation, alpha-Helical; Protein Engineering; protein folding; Proteins; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Research Communications; RNA-Binding Proteins - chemistry; RNA-Binding Proteins - genetics; RNA-Binding Proteins - metabolism; Rop protein; Sequence Inversion; sequence–structure relationship; X-Ray Diffraction; sequence–structure relationship; Rop protein; heptad repeat; protein folding; hyperthermophilic protein

Earlier studies have found that the occurrence of inverse sequence identity in proteins is not indicative of three‐dimensional similarity, but rather leads to different folds or unfolded proteins. Short helices, however, frequently keep their conformations when their sequences are inverted. To explo...