Major increase in endopeptidase activity of human cathepsin B upon removal of occluding loop contacts

NMR signal detection was utilized to site an evidence of side-to-side interactions among isolated transmembrane domains of the EGF receptor as a class I receptor tyrosine kinase. The transmembrane domain of the EGF receptor displays a low density to formation of homodimers/oligomers in fluid phospholipid membranes. Peptide-peptide interactions were detected through their effects on the backbone motion and conformation.