Fine structure of a membrane anchor domain.

摘要: Abstract We describe a detailed deletion analysis of the anchoring domain model membrane protein. Removal 23 contiguous uncharged amino acids from carboxy terminus bacteriophage f1 gene III protein (pIII) converts it an integral to secreted periplasmic form. Deletions that remove six or fewer residues hydrophobic core result in no diminution protein's capacity anchor membrane. Longer deletions into this gradually destabilize protein-membrane association. pIII derivatives with over half deleted retain substantial residual function. The basic residues, arginine and lysine, which provide carboxy-terminal boundary for domain, can be without loss capacity.