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MCAT Biochemistry > Proteins > Flashcards

Proteins Flashcards

(56 cards)

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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,

Study These Flashcards
A

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

24
Q

Agglutination

Study These Flashcards
A

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

25
Agglutination clinical uses
blood typing and pregnancy tests
26
How do antibodies recognize antigens?
through their specificity
27
Antigen binding site formation
formed through the variable regions of the heavy and light chains of the immunoglobulin
28
Protein Denaturation
disruption of protein folding by chemicals/solvents, temperature (irreversible), or pH
29
Protein denaturation characteristics
disrupts the 3D structure without breaking peptide bonds (secondary, tertiary, and quaternary),
30
Protein Renaturation
can sometimes occur after the denaturant is removed
31
Structural Protein examples
cytoskeleton, anchoring proteins, extracellular matrix, collagen, elastin, keratin, actin, tubulin,
32
Hydrophobic Effect
protein folding is spontaneous and folds so that hydrophobic residues are oriented inward,
33
Motor Protein examples
myosin, dynein, kinesin,
34
kinesin
anterograde transport - kinesin travels away from the nucleus, along microtubules
35
dynein
retrograde transport - dynein travels toward the nucleus, along microtubules
36
myosin
travels along thin filaments (actin),
37
CEKAT (structural proteins)
collagen elastin keratin actin tubulin
38
Motor Protein mnemonic
dynein drags in (retrograde) kinesin kicks out (anterograde)
39
Collagen
most abundant body protein, provides structural support and strength, long and fibrous, forms a triple helix for stability
40
Elastin
provides elasticity to skin, lungs, and blood vessels, elastin molecules are cross-linked to form a network that can stretch without breaking,
41
Keratin
fibrous protein that provides mechanical strength and protection to epithelial cells, cross-linking of alpha-helix proteins to provide unique mechanical properties,
42
Actin
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
Tubulin
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
Motor Proteins
use energy from ATP hydrolysis to move along cytoskeletal tracks and transport molecules and organelles within cells
45
Myosin
motor protein involved in muscle contraction, cytokinesis, and intracellular transport, myosin head interacts with actin and tail binds to cargo
46
Kinesin (anterograde)
motor protein involved in intracellular transport, two globular heads that interact with microtubules and a tail that binds to cargo molecules,
47
Kinesin during cell division
interacts with microtubules and pulls chromosomes towards cell poles during anaphase
47
Dynein (retrograde)
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
Binding Proteins
proteins that specifically bind to other molecules, involved in oxygen transport, signal transduction, gene regulation
48
Hemoglobin
binding protein that binds to oxygen in lungs and releases in the tissues, tetrametric protein composed of two alpha and two beta subunits,
49
Calcium-Binding Protein
binding protein acts in signal transduction, muscle contraction, and intracellular transport, bind to calcium ions and induce a conformational change,
50
DNA-Binding Protein
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
Cell Adhesion Molecules (CAMs)
involved in the binding or cells to one another or the extracellular matrix, roles in cell mitigation, tissue development, and immune responses,
52
Cadherins
CAMs involved in cell-cell adhesion, cadherins bind to other cadherins on adjacent cells through homophilic reactions,
53
Integrins
CAMs involved in cell-ECM adhesion, integrins bind to ECM proteins through heterophilic interactions, regulates in cell migrations, proliferation, and differentiation
54
Selectins
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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