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A homotetramer is a protein complex made up of four identical subunits which are associated but not covalently bound. [3] Conversely, a heterotetramer is a 4-subunit complex where one or more subunits differ. [4] Examples of homotetramers include: enzymes like beta-glucuronidase (pictured) export factors such as SecB from Escherichia coli [5]
Structure of a G-quadruplex. Left: a G-tetrad. Right: an intramolecular G4 complex. [1]: fig1 In molecular biology, G-quadruplex secondary structures (G4) are formed in nucleic acids by sequences that are rich in guanine. [2] They are helical in shape and contain guanine tetrads that can form from one, [3] two [4] or four strands. [5]
Protein tertiary structure is the three-dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains and the backbone may interact and bond in a number of ways. The interactions and bonds of side chains within a ...
Protein before and after folding Results of protein folding. Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure. This structure permits the protein to become biologically functional. [1]
A structural domain is an element of the protein's overall structure that is self-stabilizing and often folds independently of the rest of the protein chain. Many domains are not unique to the protein products of one gene or one gene family but instead appear in a variety of proteins.
The anchorage of the cytoskeleton to the chromosomes takes place at the centromere thanks to a protein complex called kinetochore. This tension results in the alignment of the bivalent at the center of the cell, the chiasmata and the distal cohesion of the sister chromatids being the anchor point sustaining the force exerted on the whole structure.
For example, standing on one leg or walking on an uneven surface both rely on your core to keep you upright and stable. Movement in all directions: While stability is crucial, your core also needs ...
Pyruvate kinase, a protein with three domains (In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of ...