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The Amino Acid Sequence of the Qß Coat Protein

Tetsuo Maita 1 and William Konigsberg 1

From the 1 From the Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510

The amino acid sequence of the coat protein from the RNA bacteriophage Qß has been determined. Tryptic peptides which were obtained from the oxidized protein accounted for all of the amino acid residues in the protein. The sequence of the tryptic peptides was established by a combination of enzymatic fragmentation and Edman degradation. The tryptic peptides were ordered on the basis of overlap peptides obtained from chymotrypsin and thermolysin digests of the protein. The Qß coat protein contains 131 residues, 2 more than the f2 or R17 coat proteins. The f2 and Qß coat proteins have only 30 residues in common, even if five insertions and five deletions are allowed in the comparison. The regions of identity are clustered in intermittent stretches 3 to 5 residues in length near the middle of the sequence.

Submitted on March 29, 1971


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