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MCAT Biochemistry > Proteins > Flashcards

Proteins Flashcards

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MCAT flashcards
1
Q

Peptide Bond (Protein Bond) Formation

A

Amide - made from an addition reaction, dehydration reaction, required a catalyst

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2
Q

Common Peptide Bond Enzyme

A

Peptidyl Transferase

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3
Q

Peptide Bond Characteristics

A

trigonal planar (cannot be rotated), resonance stabilized,

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4
Q

Peptide Bond (Protein Bond) Hydrolysis Requirements

A

requires enzymes, proteases, acids, or high temperatures,

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5
Q

Polypeptide Synthesis

A

AA through dehydration, facilitated by ribosomes in translations

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6
Q

proteins

A

one or more polypeptide molecules, 3D conformation, active sites, structures for function

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7
Q

Primary Structure

A

AA sequence in a linear form, bonds/IMF

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8
Q

Secondary Structure

A

alpha helix, beta pleated sheet,
hydrogen bonds, prevalent in structural proteins, 3D folding of the linear peptide chain

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9
Q

Beta Pleated Sheet Forms

A

Anti - N/C more stable
Parallel - N/N less stable

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10
Q

Alpha helices

A

3.6 residues per turn,

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11
Q

Beta Pleated Sheet turns

A

4 AAs,
1. Any
2. Proline (makes kink)
3. Glycine (flexible, makes turn)
4. Any

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12
Q

Tertiary Structure

A

3D shape of polypeptide at its most stable, folding is due to side chain interactions

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13
Q

Tertiary interactions

A
  1. Hydrophobic Interactions between R groups
  2. Hydrogen Bonding
  3. Ionic Bonding (ASP/LYS)
  4. Disulfide Bonds (cysteine)
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14
Q

Covalent tertiary Interactions

A

Disulfide Bonds

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15
Q

Noncovalent tertiary interactions

A

polar/polar, nonpolar/hydrophobic, h-bonds, ionic bonds

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16
Q

Structural proteins

A

fibrous,

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17
Q

Enzymatic Proteins

A

globular,

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18
Q

Quaternary Structure

A

2 of more polypeptides are combined, includes polypeptides and ligands,

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19
Q

Quaternary Characteristics

A

polar R groups are exposed, nonpolar R groups are hidden,

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20
Q

Immunoglobulins (antibodies)

A

produced by B cells in response to antigens, recognizing and neutralizing pathogens,

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21
Q

Immunoglobulins structure

A

Y shaped, made up of 4 polypeptide chains (2 heavy and 2 light), chains are linked by disulfide bonds and non-covalent interactions,

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22
Q

Antigen

A

molecules or structures identified by the immune system as foreign,

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23
Q

Antigen neutralization mechanisms,

A

complement activation,
opsonization,
antibody-dependent cell-mediate cytotoxicity

24
Q

Agglutination

A

cross-linking of antigens by antibodies to form large insoluble complexes, neutralizes pathogens and facilitates their clearance by the immune system

25
Q

Agglutination clinical uses

A

blood typing and pregnancy tests

26
Q

How do antibodies recognize antigens?

A

through their specificity

27
Q

Antigen binding site formation

A

formed through the variable regions of the heavy and light chains of the immunoglobulin

28
Q

Protein Denaturation

A

disruption of protein folding by chemicals/solvents, temperature (irreversible), or pH

29
Q

Protein denaturation characteristics

A

disrupts the 3D structure without breaking peptide bonds (secondary, tertiary, and quaternary),

30
Q

Protein Renaturation

A

can sometimes occur after the denaturant is removed

31
Q

Structural Protein examples

A

cytoskeleton, anchoring proteins, extracellular matrix, collagen, elastin, keratin, actin, tubulin,

32
Q

Hydrophobic Effect

A

protein folding is spontaneous and folds so that hydrophobic residues are oriented inward,

33
Q

Motor Protein examples

A

myosin, dynein, kinesin,

34
Q

kinesin

A

anterograde transport - kinesin travels away from the nucleus, along microtubules

35
Q

dynein

A

retrograde transport - dynein travels toward the nucleus, along microtubules

36
Q

myosin

A

travels along thin filaments (actin),

37
Q

CEKAT (structural proteins)

A

collagen
elastin
keratin
actin
tubulin

38
Q

Motor Protein mnemonic

A

dynein drags in (retrograde)
kinesin kicks out (anterograde)

39
Q

Collagen

A

most abundant body protein, provides structural support and strength, long and fibrous, forms a triple helix for stability

40
Q

Elastin

A

provides elasticity to skin, lungs, and blood vessels, elastin molecules are cross-linked to form a network that can stretch without breaking,

41
Q

Keratin

A

fibrous protein that provides mechanical strength and protection to epithelial cells, cross-linking of alpha-helix proteins to provide unique mechanical properties,

42
Q

Actin

A

protein that forms myofilaments to provide maintenance of cell shape and formation of cell structures, forms linear filaments which provide cells with the ability to change shape and move

43
Q

Tubulin

A

forms microtubules, important for transport, cell division, and maintenance of shape, involved in the formation of cilia and flagella, formed by polymerization of alpha- and beta-tubulin dimers,

44
Q

Motor Proteins

A

use energy from ATP hydrolysis to move along cytoskeletal tracks and transport molecules and organelles within cells

45
Q

Myosin

A

motor protein involved in muscle contraction, cytokinesis, and intracellular transport, myosin head interacts with actin and tail binds to cargo

46
Q

Kinesin (anterograde)

A

motor protein involved in intracellular transport, two globular heads that interact with microtubules and a tail that binds to cargo molecules,

47
Q

Kinesin during cell division

A

interacts with microtubules and pulls chromosomes towards cell poles during anaphase

47
Q

Dynein (retrograde)

A

motor protein involved in intracellular transport, two heavy chains that form the motor domain, two intermediate chains with light chains to interact with cargo,

47
Q

Binding Proteins

A

proteins that specifically bind to other molecules, involved in oxygen transport, signal transduction, gene regulation

48
Q

Hemoglobin

A

binding protein that binds to oxygen in lungs and releases in the tissues, tetrametric protein composed of two alpha and two beta subunits,

49
Q

Calcium-Binding Protein

A

binding protein acts in signal transduction, muscle contraction, and intracellular transport, bind to calcium ions and induce a conformational change,

50
Q

DNA-Binding Protein

A

binds to DNA, including transcription factors and histones, play role in gene regulation and chromatin structure, binds to specific sequences through hydrogen bonding, electrostatic interactions, and hydrophobic interactions,

51
Q

Cell Adhesion Molecules (CAMs)

A

involved in the binding or cells to one another or the extracellular matrix, roles in cell mitigation, tissue development, and immune responses,

52
Q

Cadherins

A

CAMs involved in cell-cell adhesion, cadherins bind to other cadherins on adjacent cells through homophilic reactions,

53
Q

Integrins

A

CAMs involved in cell-ECM adhesion, integrins bind to ECM proteins through heterophilic interactions, regulates in cell migrations, proliferation, and differentiation

54
Q

Selectins

A

CAMs involved in leukocyte adhesion and recruitment to sites of inflammation, binds to carbohydrates on the surface of leukocytes and endothelial cells through heterophilic reactions

MCAT Biochemistry (2 decks)

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