SC BIOL 620 - Secondary Structure of Hemoglobin (3 pages)

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Secondary Structure of Hemoglobin



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Secondary Structure of Hemoglobin

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Lecture number:
6
Pages:
3
Type:
Lecture Note
School:
University Of South Carolina-Columbia
Course:
Biol 620 - Immunobiology

Unformatted text preview:

BIOL 620 1st Edition Lecture 6 Outline of Current Lecture Immunology Secondary Structures of hemoglobin molecule Current Lecture Allotype Variations outside the motifs gives allotype Allotype with isotype has slight amino acid variation within alleles Same isotype can have idiotype but not necessary Same allotype does not mean the same idiotype Domains There are intra chain disulphide bonds as well as inter chain disulphide bonds with light chain and heavy chain Sequence amino acids in each domain CH 1 125 amino acids CH 2 375 nucleotides Due to repeated mutations in ancestral genome there are 3 sequences coding for related proteins There is immunoglobulin supergene family Biological functions of domains Variable Domain binds to Ag CH1 serves as a arm to extend Ag binding site also donates cysteine to form disulphide bridge between heavy and light chain Stabilizes Variable light and Variable constant interaction Adds to Ab diversity Hinge region gives flexibility to arms twists at hinge region Rich in proline and cysteine whereby proline gives turn in hexagon structure Ig M and Ig E has no hinge region CH 1 takes over this role to Ab arm flexibility CH 2 Domain Resolves Ab in water Since Aqueous form nedded for serum Globular protein dissolves well Long peptides have lesser dissolution CH 2 region has amino acids with carbohydrate oligosaccharide side chains which push CH 2 domains apart and enhance solubility Complement activation CH 3 enhances phagocytic binding active role in opsonization and enhanced binding for phagocytosis when Ab is attached to Ag Isotypes Features and Functions Ig G 4 different gamma chains in genome 4 different Ig G subtypes vary in hinge region and number of disulphide bonds Ig G1 Ig G3 Ig G4 can cross the placenta Ig G3 and Ig G 1 activate complements Also Ig G3 has the strongest complement activation Ig G1 and Ig G3 bind to Fragment C receptors The Fragment C receptors bind to Fragment C fragment of Ig G molecule Ig M found in the



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