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The water-accessible surface area of an IgG antibody. Immunoglobulin G (IgG) is a type of antibody. Representing approximately 75% of serum antibodies in humans, IgG is the most common type of antibody found in blood circulation. [1] IgG molecules are created and released by plasma B cells. Each IgG antibody has two paratopes.
structure summary The immunoglobulin domain , also known as the immunoglobulin fold, is a type of protein domain that consists of a 2-layer sandwich of 7-9 antiparallel β-strands arranged in two β-sheets with a Greek key topology, [ 1 ] [ 2 ] consisting of about 125 amino acids.
Antibody (or immunoglobulin) structure is made up of two heavy-chains and two light-chains.These chains are held together by disulfide bonds.The arrangement or processes that put together different parts of this antibody molecule play important role in antibody diversity and production of different subclasses or classes of antibodies.
In IgG, IgA and IgD antibody isotypes, the Fc region is composed of two identical protein fragments, derived from the second and third constant domains of the antibody's two heavy chains; IgM and IgE Fc regions contain three heavy chain constant domains (C H domains 2–4) in each polypeptide chain.
The framework regions are highly conserved regions of the variable portion of the antibody. The evolutionary reason for the conservation of these regions is to support proper folding of the antibody allowing the CDR regions to be stabilized. Folding in FR leads to antibody structure flexibility or rigidity of the binding region of the antibody ...
Sulesomab, an antigen that recognizes proteins on the surface of granulocytes, is used to label out infections, again using the 99m Tc isotope. [ 7 ] Fab fragments are often fused to small proteins (<100 kDa) that have lower scattering, resulting in images with less contrast.
Protein G is an immunoglobulin-binding protein expressed in group C and G streptococcal bacteria much like protein A but with differing binding specificities. It is a ~60-kDA (65 kDA for strain G148 and 58 kDa for strain C40) [ 1 ] cell surface protein that has found application in purifying antibodies through its binding to the Fab and Fc region.
Ribbon diagrams, also known as Richardson diagrams, are 3D schematic representations of protein structure and are one of the most common methods of protein depiction used today. The ribbon depicts the general course and organisation of the protein backbone in 3D and serves as a visual framework for hanging details of the entire atomic structure ...