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2011_09_23_Quaternary_structure_and_classification

2011_09_23_Quaternary_structure_and_classification -...

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Structural Organization of Proteins
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Quaternary structure Quaternary structure is the spatial arrangements of subunits (i.e. each polypeptide chain) and the nature of their interactions - mainly driven by hydrophobic interactions Monomer, dimer , trimer, tetramer , pentamer, hexamer, heptamer, ocatmer, decamer, dodecamer, viral - often arranged symmetrically Molecular machines are often multimers, eg. proteosome = 4 heptameric rings (28-mer), ribosome (protein + RNA) Also have multiprotein complexes (more than one protein comes together to form a stable complex via protein-protein interactions) roles of quaternary structure: - Control or regulation – allostery or cooperativity - Stability - Partial active sites – eg. 2 subunits are required for the full active site
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mild denaturation 2 2 2 ! ! " ! " ! " " contains 2( "! ) identical subunits contains 4 subunits( " or ! ) more drastic denaturation Quaternary structure analyses complete denaturation 4 chains (random coils) + 4 heme Quaternary structure analysis: MW of native oligomer
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