BIOC 3560 Study Guide - Final Guide: Immunoglobulin Light Chain, Cyclin-Dependent Kinase 2, Catalytic Triad
6 Apr 2016
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Document Summary
Hemoglobin is a tetramer, has a quaternary structure. Primary structures are largely dissimilar (with some key invariant amino acids that make the secondary and tertiary structures very similar) Both can be bound to co because of heme. Hb is capable of cooperative binding and conformational change. Curve of myoglobin binding oxygen is hyperbolic while the curve of hemoglobin binding oxygen is sigmoidal. Carboxy termini of heavy chains form left-handed coil-coil. Amino termini, heavy chain has domain containing atpase activity. In muscle cells, myosin molecules form thick filaments. Globular monomers (g-actin) polymerize to form long filaments (f-actin) Myosin thick filaments and f-actin thin filaments to form myofibrils within a muscle cell (fibre) In muscle cells, thin filaments are made up of f-actin along with tropomyosin and troponin. Change in quaternary structure causes allosteric effects in atcase. Atcase has a more closed conformation in the t state.
