Structure and Stability of Recombinant Protein Depend on the Extra N-terminal Methionine Residue: S6 Permutein from Direct and Fusion Expression Systems
Permuted Protein, Recombinant Protein, Protein Structure, Conformational Stability
Digital Object Identifier (DOI)
Two permuted variants of S6 ribosomal protein were obtained in direct and fusion expression systems, respectively. The product of direct expression contained the extra N-terminal methionine residue. The structural properties and conformational stability of these permuteins were compared using 1-D 1H-NMR, circular dichroism, intrinsic fluorescence, differential scanning calorimetry and resistance to urea-induced unfolding. A pronounced difference in all the parameters studied has been demonstrated. This means that the structure of recombinant protein can be sensitive to peculiarities of the expression and purification procedures, leading particularly to the presence or absence of the Met at the first position in the target protein sequence.
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Citation / Publisher Attribution
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, v. 1432, issue 2, p. 324-332
Scholar Commons Citation
Uversky, Vladimir N.; Abdullaev, Ziedulla Kh.; Arseniev, Alexander S.; Bocharov, Eduard V.; Dolgikh, Dmitry A.; Latypov, Ramil F.; Melnik, Tatiana N.; Vassilenko, Konstantin S.; and Kirpichnikov, Mikhail P., "Structure and Stability of Recombinant Protein Depend on the Extra N-terminal Methionine Residue: S6 Permutein from Direct and Fusion Expression Systems" (1999). Molecular Medicine Faculty Publications. 651.