Structure of rabbit skeletal myosin: Analysis of the amino acid sequences of two fragments from the rod region

摘要: Abstract The amino acid sequences of fragments from light meromyosin and heavy subfragment-2 have been analysed structural features noted. As with other α-fibrous protein sequences, there is a regular disposition apolar residues in positions d the heptapeptide-type repeat characteristic coiled-coil conformation. common occurrence acidic basic e g positions, respectively, give rise to maximum number interchain ionic interactions when two parallel chains myosin are axial register. Although quasi-repeating heptapeptides both points discontinuity (unlike that most proteins), secondary structure prediction methods indicate will be 90 100% α-helical. Fast Fourier transform techniques revealed significant periodicity about 27.4 ± 0.3 (~41 A) linear fragments. This period compatible similarly directed molecules thick filament being axially staggered respect one another by an odd multiple 143 A. Preliminary evidence also presented show sequence rod region may 28 residue gene duplication repeat.