Search results
Results from the WOW.Com Content Network
The Titin protein is located between the myosin thick filament and the Z disk. [25] Titin consists primarily of a linear array of two types of modules, also referred to as protein domains (244 copies in total): type I fibronectin type III domain (132 copies) and type II immunoglobulin domain (112 copies).
The main proteins involved are myosin, actin, and titin. Myosin and actin are the contractile proteins and titin is an elastic protein. The myofilaments act together in muscle contraction, and in order of size are a thick one of mostly myosin, a thin one of mostly actin, and a very thin one of mostly titin. [1] [2]
Ribbon diagram of myoglobin bound to haem (sticks) and oxygen (red spheres) (Ribbon diagrams, also known as Richardson diagrams, are 3D schematic representations of protein structure and are one of the most common methods of protein depiction used today. The ribbon depicts the general course and organization of the protein backbone in 3D and ...
A diagram of the structure of a myofibril (consisting of many myofilaments in parallel, and sarcomeres in series) Sliding filament model of muscle contraction. The myosin heads form cross bridges with the actin myofilaments; this is where they carry out a 'rowing' action along the actin. When the muscle fibre is relaxed (before contraction ...
The protein is known to sever actin filaments by creating more positive ends on filament fragments. [4] Cofilin/ADF (destrin) is likely to sever F-actin without capping [ 6 ] and prefers ADP-actin. These monomers can be recycled by profilin , activating monomers to go back into filament form again by an ADP-to- ATP exchange.
At the top level are all alpha proteins (domains consisting of alpha helices), all beta proteins (domains consisting of beta sheets), and mixed alpha helix/beta sheet proteins. While most proteins adopt a single stable fold, a few proteins can rapidly interconvert between one or more folds. These are referred to as metamorphic proteins. [5]
Myomesin is bound to myosin at its N-terminal. Obscurin connects the myomesin dimers and binds to the C-terminal of titin. It is thought that the myomesin-titin interaction is vital for the execution of the mechanical functions of the Ser/Thr kinase domain of titin. [2] Myomesin is a protein family found in the M-line of the sarcomere structure.
Although the ribbon cartoon is the most common way of displaying a protein structure, a protein whose surface shape clearly affects its function may best be shown as a surface. For example, a surface representation may help demonstrate the contours of a binding pocket or size of a membrane protein pore.