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Titin is the third most abundant protein in muscle (after myosin and actin), and an adult human contains approximately 0.5 kg of titin. [13] With its length of ~27,000 to ~35,000 amino acids (depending on the splice isoform ), titin is the largest known protein . [ 14 ]
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] Types of muscle tissue are striated skeletal muscle and cardiac muscle, obliquely striated muscle (found in some invertebrates), and non-striated smooth muscle. [3]
Intermediate filaments (IFs) are cytoskeletal structural components found in the cells of vertebrates, and many invertebrates. [1] [2] [3] Homologues of the IF protein have been noted in an invertebrate, the cephalochordate Branchiostoma.
When a cell is in the interphase process, microtubules tend to all orient the same way. Their negatively charged end will be close to the nucleus of the cell, while their positively end will be oriented away from the cell body. The basal body found within the cell helps the microtubule to orient in this specific fashion.
Proteins make up half the dry weight of an Escherichia coli cell, whereas other macromolecules such as DNA and RNA make up only 3% and 20%, respectively. [58] The set of proteins expressed in a particular cell or cell type is known as its proteome. [54]: 120 The enzyme hexokinase is shown as a conventional ball-and-stick molecular model.
Myotilin is a structural protein that, along with titin and alpha-actinin give structural integrity to sarcomeres at Z-discs in striated muscle. Myotilin induces the formation of actin bundles in vitro and in non-muscle cells.
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.
cMyBP-C is a 140.5 kDa protein composed of 1273 amino acids. [7] [8] [9] cMyBP-C is a myosin-associated protein that binds at 43 nm intervals along the myosin thick filament backbone, stretching for 200 nm on either side of the M-line within the crossbridge-bearing zone (C-region) of the A band in striated muscle. [10]