Abstract
Chymotryptic peptides of CGMMV protein were separated by chromatography on a AG50W-X2 column. Tryptic peptides obtained before and chymotryptic peptides which contain basic amino acids were aligned to yield a partial amino acid sequence (residue 41 to 129 in the corresponding TMV protein) of the protein. Amino acid sequences of coat proteins of TMV group were compared and CGMMV protein showed some variations even in such sections as 87 to 94 or 113 to 122, which is identical in the other coat proteins. Distributions of hydrophobicity in CGMMV, TMV, and HR proteins were found to be very similar each other in spite of fairly large difference in amino acid sequences. This suggests that the specific distribution of hydrophobicity in the primary structure would be significant for specific conformation of the protein which construct the rod-shaped virus particle.
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