van Beynum G M, de Graaf J M, Castel A, Kraal B, Bosch L
Eur J Biochem. 1977 Jan 3;72(1):63-78. doi: 10.1111/j.1432-1033.1977.tb11225.x.
The complete amino acid sequence of the coat protein of alfalfa mosaic virus (strain 425) is reported. Sequence determinations were mainly performed on peptides obtained from fragmentation by cyanogen bromide and trypsin. Both manual and automatic sequence methods were used. Some refinements of the solid-phase Edman degradation were introduced. The final alignment of the peptides was established by means of alternative cleavage methods, such as limited tryptic digestion of intact virus particles, tryptic digestion after blockage of lysine residues and chymotryptic digestion. The coat protein consists of 220 amino acid residues corresponding to a molecular weight of 24252. A remarkable clustering of basic residues occurs in the N-terminal part of the protein chain. Several internal hydrophobic clusters and a strongly acidic site at the C-terminus can be observed. Two regions of sequence homology (12 residues) were found. Some features of the secondary structure are predicted.
报道了苜蓿花叶病毒（425株系）外壳蛋白的完整氨基酸序列。序列测定主要针对由溴化氰和胰蛋白酶裂解得到的肽段进行。同时使用了手动和自动测序方法。对固相埃德曼降解法进行了一些改进。通过其他裂解方法，如对完整病毒颗粒进行有限的胰蛋白酶消化、赖氨酸残基封闭后的胰蛋白酶消化和胰凝乳蛋白酶消化，确定了肽段的最终排列。外壳蛋白由220个氨基酸残基组成，分子量为24252。在蛋白质链的N端部分，碱性残基显著聚集。可以观察到几个内部疏水簇以及C端的一个强酸性位点。发现了两个序列同源区域（12个残基）。预测了二级结构的一些特征。
