This section describes an example of how the form of structural proteins relates to motion: namely the contraction of skeletal muscle .
Other examples to investigate include:
(Here are links to the course pages dealing with microtubules , membrane proteins , fibrous proteins )
Skeletal muscles (also called striated or striped muscle) are only one type of muscle tissue occurring in vertebrates. They are generally under voluntary control. The other two are (i) cardiac (i.e. heart) muscle, which is specialized but resembles skeletal muscle in many respects, and (ii) smooth muscle which is generally controlled involuntarily by the autonomic nervous system .
Skeletal muscle cells are highly specialized. They are called myofibres, cylindrical in shape, 0.01 - 0.05 mm in diameter and 1 - 40 mm long. These multinucleate cells consist of a bundle of myofibrils surrounded by a plasma membrane. A muscle consists of a bundle of myofibres.
A myofibril consists of repeating identical units called sarcomeres. Regular repeating formations of two types of protein filaments are the basis of the sarcomere:
The structure of the sarcomere is described on the next page.
A single myosin molecule consists of two heavy chains and four light chains. It is effectively a dimer of two heterotrimers, each of which consists of two different light chains (approximately 20 kD in mass) and a single heavy chain (230 kD). The latter has a globular head and a long alpha-helical tail. In fact the two tails of the complete molecule form a parallel coiled-coil, so that myosin consists of a long (1500 Å) fibre, 20 Å thick, with a two-headed globular end. There is a hinge region between each head and the tail section.
Here is a diagram. (5Kb)
A myosin molecule has three functions:
The two different structural domains are responsible for different functions, as is revealed by treatment of myosin with proteases to give different subunits. Cleavage of myosin with trypsin gives two products:
Treatment of HMM with the protease papain cleaves the two globular heads from the tail section (S2). The two heads (termed S1) are not surprisingly found to be the site of ATPase activity; they also bind to actin filaments.
Click here for the crystal structure (C-alpha atoms only) of a proteolytic fragment of myosin from chicken muscle. 1mys (100Kb) [Bbk|BNL|ExP|Waw|Hal]
This fragment consists of an entire S1 head (843 residues) and two light
Diagram. (16Kb) To achieve this rendition, colour the molecule by 'chain' and select 'spacefill' from the menu.
This fragment (all atoms) contains
two light chains and 60 residues of the heavy chain.
1scm (238Kb) [Bbk|BNL|ExP|Waw|Hal] Diagram. (12Kb)
Myosin is therefore unusual in that it is both a fibrous protein, and a globular enzyme.
Thick filaments consist almost entirely of myosin. A myosin filament contains several hundred myosin molecules in two bundles packed end to end. In each bundle, the myosin molecules all point in the same direction, giving an aggregation of the myosin tails with the globular heads protruding in a regular helical arrangement. The two bundles are packed such that the ends of the tails are facing each other, but the tails from one bundle overlap those of the other, so that the "bare zone" where there are no S1 heads is less than twice the length of a single myosin tail.
Here is a diagram.
Last updated 16th April '97