Nuclear magnetic resonance evidence for a flexible region at the C-terminus of alpha-tropomyosin.
The 1H nuclear magnetic resonance spectrum of alpha-tropomyosin contains a number of sharp peaks indicative of the presence of small regions of high flexibility in the molecule. Removal of 9 to 11 residues from the C-terminus by digestion with carboxypeptidase A causes a marked decline in the intensity of these peaks. The difference is consistent with at least the C-terminal four residues of the sequence (-Met-Thr-Ser-Ile) being highly mobile. The conformation of the C-terminus is thus radically different from the alpha-helical coiled-coil from which the bulk of the molecule is constructed.
D002268:Carboxypeptidases / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D014335:Tropomyosin
D014335:Tropomyosin; D002268:Carboxypeptidases