antibody structure and function Flashcards
why are antibodies also called globular proteins and immunoglobulins?
because they are large glycoproteins based on their tertiary and quaternary structure have globular confirmation
what is the simplest antibody composed of?
4 peptide chains with an amino and carboxyl end bound together by disulfide bonds
what are the Fab regions of the antibody?
amino ends of the polypeptide sites
what is in the Fc region of the antibody?
carboxyl ends of the peptides
what are the two forms of light chains?
lambda and kappa ends
true or false: Since the chains are identical on an antibody molecule, an antibody will contain either forms of the light chains
true
what proteolytic enzyme was Porter working with?
papain
what does papain chemically digest an antibody molecule into and the significance of it?
3 proteins
Two of them were able to still bind antigen epitope and labeled them Fragment antigen binding (Fab) and the last could be crystalized out of solution (Fc).
what can digest the antibody molecule in to a divalent fragment (F(ab’)2) and numerous Fc
smaller fragments?
endopeptidase pepsin
what part of the antibody determines the antigenic epitope specificity of each antibody?
the 2 light polypeptide chains and 2 heavy polypeptide chains of the V regions
what impacts the structural conformation of the regions of 2 light polypeptide chains and 2 heavy polypeptide chains (V regions)?
they have a high degree of variability of amino acid sequences
true or false: for each antibody the 2 heavy
polypeptide chains and the 2 light chains are different to each other.
false: identical
why is the C region called the constant regions?
the light polypeptide chains and heavy chains contain relatively conserved amino acids for the individual
what is the purpose of the hinge region?
provide flexibility to the antibody molecule aiding in its function
antibodies can be bound to the surface of B cells as a component of the B cell receptors (BCR) coupled with a ____________________________ to form the B cell receptor complex
surface heterodimer protein Igα/Igβ
when antibodies exist as a secretory protein, where can they be found?
secretions, intracellular spaces, and blood vascular
true or false: each antibody has specificity for a particular antigenic epitope
true
what is the specificity of the antibody conserved for?
all the BCRs on that specific B cell and all the antibodies that are produced by that specific B cell
what is the hypervariable regions of the antigen-antibody binding (Fab) region?
complimentary determining regions (CDRs) in which the amino acids in these regions are unique per antibody
what is the result of the substitution of the amino acids in the CDR?
alter the structural conformation of the antibody binding site and thus, the antigenic epitope that it can recognize
what solely defines the conformational groove that recognizes a specific epitope structure?
based on the interaction between the amino acid sequences in the hypervariable regions or CDRs of the heavy chain with the CDRs of the light chain
what is the outcome of the hypervariable region?
each naïve B cell can create an antibody with a
unique antibody binding site capable of recognizing a unique antigen epitope
what does the cysteine contain that forms the disulfide bonds between the peptide chains?
reactive sulfhydryl groups
the hinge region of the heavy chains allow for what?
flexibility for optimal binding to multiple antigens expressing the same epitope