Antibodies Intro Flashcards

1
Q

What are antibodies?

A

Glycoproteins produced by B cells that bind specifically to antigens and target them for destruction

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2
Q

What are the basic components of an antibody?

A

Two identical heavy chains and two identical light chains held together by disulfide bonds

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3
Q

What are the two functional regions of an antibody?

A

Fab region that binds antigen and Fc region that interacts with the immune system

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4
Q

What is the role of the hinge region in an antibody?

A

Provides flexibility for binding multiple antigens

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5
Q

What are variable and constant regions in an antibody?

A

Variable regions bind to antigens while constant regions determine the antibody class and immune system interactions

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6
Q

What are hypervariable regions HVRs?

A

Specific parts of the variable regions that bind to antigens also known as complementarity-determining regions CDRs

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7
Q

What is an antigen?

A

A molecule that triggers an immune response by generating antibodies

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8
Q

What is an epitope?

A

The specific part of the antigen that an antibody binds to

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9
Q

How do antibodies bind antigens?

A

Through non-covalent interactions like hydrogen bonds ionic bonds and Van der Waals forces

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10
Q

What is antibody affinity?

A

The strength of interaction between a single antigen binding site and its antigen

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11
Q

What is antibody avidity?

A

The overall strength of binding between an antibody and a multivalent antigen

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12
Q

How do IgG and IgM differ in binding strength?

A

IgG’s bivalency increases avidity by about 10^4 while IgM’s pentameric structure increases it by about 10^7

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13
Q

What does divalent mean in relation to antibodies?

A

It refers to antibodies like IgG having two antigen binding sites

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14
Q

What are multimeric antigens?

A

Antigens with multiple or repeated epitopes

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15
Q

What are the key molecular forces in antigen-antibody interactions?

A

Hydrogen bonds ionic bonds hydrophobic interactions and Van der Waals forces

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16
Q

What are the two main uses of antibodies in research?

A

Detecting and purifying proteins such as through primary and secondary antibody systems

17
Q

What is the function of complementarity-determining regions CDRs?

A

To form the antigen-binding site by creating a complementary shape to the antigen

18
Q

What is the difference between affinity and avidity?

A

Affinity is the strength of one binding site interaction while avidity is the cumulative strength of all interactions

19
Q

What determines the strength of an antibody-antigen interaction?

A

The fit and summation of non-covalent forces at the binding site

20
Q

What are camelid antibodies and why are they significant?

A

Camelid antibodies are smaller preserving their binding ability while reducing immunogenicity making them useful in therapeutic applications