Biochemistry 2280A Chapter Notes - Chapter 121-141: Cyclic Adenosine Monophosphate, Cytoskeleton, Elastin

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In aqueous environments, hydrophobic molecules tend to be forced together to minimize their disruptive effect on the hydrogen-bonded network of surrounding water molecules. The -helix and the sheet are common folding patterns. Neuraminidase: consists of a ring of 4 identical protein subunits. Hemoglobin: contains 2+ different polypeptide chains (2-alpha, 2-beta subunits) Identical proteins with 2 different binding sites will often form a long, helical filament. If the 2 binding sites are disposed appropriately in relation to each other the protein subunits will form a closed ring instead of a helix. Elastin: formed from loose and unstructured polypeptide chains that covalently cross-link into rubberlike elastic meshwork. Keratin: extremely stable; dimer of 2 identical subunits, with long alpha-helices of each subunit forming a coiled-coil. These coiled-coil regions are capped at either end by globular domains containing binding sites allows them to assemble into ropelike intermediate filaments (component of cytoskeleton that gives cells mechanical strength)

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