Protein Function

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54 Semester 1 (BIOCHEM 2280) Karteikarten am Protein Function , erstellt von UdaraJay am 25/09/2015.
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Collagen They are the most common type of fibrous protein found in animals (25-30%). The connect and strengthen tissues, and have a characteristic triple helical structure.
Poly-proline type II characteristics Glycine as every third residue Lot of hydroxylated prolines and lysine
What hydroxylyzes proline and lysine prolyl hydroxylase lysyl hydroxylase
What causes scurvy A lack of vitamin c > which prevents iron from being reduces > which prevents the function of proly-hydroxylase > proline is not hydroxylised > poly-proline type II doesn't form triple helical structure
Is collagen hydrophobic? Quite hydrophobic due to the many exposed hydrophobic side chains
Ostyogenesis Imperfecta Often glycine mutations. Prevents proper assembly of triple helix. Leads to lack of collagen.
Malformed or absent bone Ehlers–Danlos syndrome (EDS) – a connective tissue disorder caused by a defect in the synthesis of collagen
Antibodies A specific protein produce by the immune system in response to a foreign molecule (antigen). They bind tightly to these antigens and mark them for destruction.
How are antibodies made? Antibodies are made by B-lymphocytes and are found in blood, lymp and other bodily fluids.
We study Immunoglobulin G or IgG Just know that.
Describe the basic structure of an antibody They are made up of 4 chains which are held together by disulphide bonds.
FC region Fragment crystallized Effector site which usually remains the same across different amino acids. -activate the complement pathway -bind to phagocytes -bind to mast cells, basophils, and eosinophils -bind to NK cells
2x FAB region fragment antigen binding They contain the antigen binding sites
Production of antibodies Created by injecting an 'antigen‘ in an animal (often rabbit, goat) After immune response, antibodies harvested from blood.
Uses of antibodies Extreme specificity makes IgG a valuable tool. 1. Lab experiments: identifying molecules 2. Clinical therapy: Anti venom 3. Clinical: diagnosis of diseases like HIV
Ligands Many proteins contain sites to which ligands specifically bind and form a “complex” with the protein. (the site is called the active site on an enzyme) Binding occurs by multiple weak or a few strong forces - leads to extreme specificity
Ligand binding - Dissociation Constant Kd High affinity = tight binding = small Kd Units are moles/L (M) (Check notes on it - the graphs are great.)
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