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Biochem > Protein Structure > Flashcards

Protein Structure Flashcards

1
Q

Protein Structure

A

amino acids and polypeptide chain

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2
Q

Polypeptide chain

A

peptide bond and phi, psi conformation

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3
Q

Monoclonal

A

-produced from single B-lymphocyte clone and bind same epitope

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4
Q

monoclonal antibodies (mAbs)

A

-used in research and therapy
-treat cancer, inflammatory disease, infectious and cardiovascular disease
-rapidly growing in use

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5
Q

OKT3

A

-first therapeutic mAb approved
-targets CD3 on T cells
-depletes T cells
-immunosuppressor in preventing transplant rejection

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6
Q

IgG antibody chains

A

-heavy and light (2 of each)
-constant or variable

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7
Q

Light chain

A

VL CL

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8
Q

Heavy chain

A

Vh3Ch

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9
Q

Ig domains

A

-Ig fold packed with hydrophobic residues (keep folded and stable)
-110-amino acids
-sandwich of 2 antiparallel sheets linked by disulfide bonds

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10
Q

Ig Fragments

A

-2 Fab regions
-Fc region

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11
Q

Fc region

A

-stem of Ig
-binds Fc receptors
-activates complement-mediated cytotoxicity

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12
Q

Full IgG antibody

A

-2 light chains with one VL and one CL
-2 heavy chains with one Vh and 3 CH’s
-2 copies of 2 chains
-Ig fold domain
-saccharide component

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13
Q

Where does the hydrolysis producing Fab and Fc occur?

A

Hinge peptide (in the middle)

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14
Q

saccharide component

A

in the constant H domains

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15
Q

IgG flexibility

A

-due to loops between Ig domains
-Fab and Fc orientation varies among Ig molecules

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16
Q

Protein function

A

dependent on binding and recognition

17
Q

molecular recognition

A

-highly specific
-complementarity
-noncovalent interactions

18
Q

Induced-fit

A

-structural changes occuring to enhance specificty and complementarity

19
Q

Variable domains

A

-comprised of 3 hypervariable loops

20
Q

Hypervariable loops

A

-comprised by variable domains
-vary in length and sequence in IgGs
-H and L chains (pic) (fab region)
-exact match between antigen and loops

21
Q

Loop matching antigen

A

-high affinity
-induced fit
-specificity

22
Q

Therapeutic Antibody mechanisms

A

-targeting extracellular ligand-receptor interactions
-antigen binding affinity is key

23
Q

Ligand-receptor interactions

A

-bind to ligand or receptor (blockade)
-can lead to receptor down regulation

24
Q

Human IgA monoclonal antibody

A

-blocks SARS-CoV-2 spike protein interaction with human ACE2 receptor
-forms MAb363 SARS-CoV-2 RBD complex

25
Q

Monoclonal IgG molecules effectively recognize one antigen with high affinity because

A

the sequences of the hypervariable loops are selected to exquisitely complement the 3D shape of the
antigen.

26
Q

Antigens are recognized with high affinity by antibodies because

A

the sequences of three hypervariable loops are selected in an immune response to exquisitely complement the 3D shape of the antigen.

27
Q

The assigned reading “Therapeutic monoclonal antibodies,” describes several types of engineered antibody molecules that have been developed for therapeutics. Which of the names below does NOT refer to a type of therapeutic monoclonal antibody?

Fab

Fc

BiTE®

scFv

A

Fc

28
Q

Twelve domains compose an IgG molecule. Of these domains,

A

all have two or more cysteine residues.

29
Q

Disulfide Bridge

A

bond between light and heavy chains of Fab

30
Q

Protease

A

-cleaves backbone
-pepsin

31
Q

pepsin

A

-protease
-cleaves hinge peptide
=2 Fab + Fc

32
Q

How many IgG domains

A

-12 domains
-4 variable (1 light, 1 heavy) x2
-8 constant (3 heavy, 1 light)x2

33
Q

Acidic Residues

A

aspartic (R), glutamic (E)

34
Q

Basic residues

A

lyseine and arginine

35
Q

receptor blockade

A

-antibody binds to receptor
-ligand cannot bind to receptor
-could lead to endocytosis and removal of cell

Biochem (30 decks)

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