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The importance of motor proteins in cells becomes evident when they fail to fulfill their function. For example, kinesin deficiencies have been identified as the cause for Charcot-Marie-Tooth disease and some kidney diseases. Dynein deficiencies can lead to chronic infections of the respiratory tract as cilia fail to function without dynein ...
Myosins (/ ˈ m aɪ ə s ɪ n,-oʊ-/ [1] [2]) are a family of motor proteins (though most often protein complexes) best known for their roles in muscle contraction and in a wide range of other motility processes in eukaryotes. They are ATP-dependent and responsible for actin-based motility. The first myosin (M2) to be discovered was in 1864 by ...
Protein domains allow protein classification by a combination of sequence, structure and function, and they can be combined in many ways. In an early study of 170,000 proteins, about two-thirds were assigned at least one domain, with larger proteins containing more domains (e.g. proteins larger than 600 amino acids having an average of more ...
As the three-dimensional structure of proteins brings with it an understanding of its function and biological context, there is great effort placed in observing the structures of proteins. X-ray crystallography was the primary method used in the 20th century to solve the structures of proteins in their crystalline form.
The generation of a protein sequence is much easier than the determination of a protein structure. However, the structure of a protein gives much more insight in the function of the protein than its sequence. Therefore, a number of methods for the computational prediction of protein structure from its sequence have been developed. [39]
Protein kinases and phosphatases work independently and in a balance to regulate the function of proteins. [3] The amino acids most commonly phosphorylated are serine, threonine, tyrosine, and histidine. [4] [5] These phosphorylations play important and well-characterized roles in signaling pathways and metabolism.
This secondary structure then folds to produce the tertiary structure of the protein. The tertiary structure is the proteins overall 3D structure which is made of different secondary structures folding together. In the tertiary structure, key protein features e.g. the active site, are folded and formed enabling the protein to function. Finally ...
The loss of these interactions alters the proteins structure, but most importantly it alters the proteins function, which can be beneficial or detrimental. A significant change in pH may even disrupt many interactions the amino acids make and denature (unfold) the protein.