Amino Acids and Proteins

Question 1

Enzymes

Answer 1

catalysts, speed the reactions up

Question 2

Hormones

Answer 2

control physiological processes

Question 3

Amylase, lipase, pepsin

Answer 3

Digestive enzyme

Question 4

Hemoglobin

Answer 4

Transport substances by blood

Question 5

Actin, tubulin, keratin

Answer 5

Structure/cytoskeleton

Question 6

Insulin, glucagon

Answer 6

Hormone signaling

Question 7

Antibodies

Answer 7

Defensive mechanism

Question 8

Myosin

Answer 8

Carry out muscle contraction

Question 9

Albumin (egg white)

Answer 9

Provide food for the embryo

Question 10

Denaturation

Answer 10

Changes in temperature or pH may disrupt protein’s shape, funtionality.

Question 11

Amino acids

Answer 11

Monomers that makeup proteins

Question 12

NH2

Answer 12

Amino group (protonated, positive charge)

Question 13

COOH

Answer 13

Carboxyl group and a hydrogen atom (deprotonated, negative charge)

Question 14

Nonpolar, Nonaromatic Amino Acids

Answer 14

Hydrophopic (hate H2O)

Question 15

Aromatic Amino Acids

Answer 15

Can absorb UV light/ determining protein concentration via spectroscopy

Question 16

Polar Uncharged Amino Acids

Answer 16

hydrophilic (H2O loving)

Question 17

Charged Amino Acids

Answer 17

Can be divided into acidic (- charged) and basic (+ charged) amino acids

Question 18

Essential Amino Acids

Answer 18

Can not be synthesized by the human body, obtained from the diet

Question 19

Non-Essential Amino Acids

Answer 19

Can be synthesized by the body

Question 20

Phosphorylation

Answer 20

Phosphate groups, signaling pathways

Question 21

Glycosylation

Answer 21

Carbohydrate groups, affecting protein folding, stability, cell recognition

Question 22

Acetylation and Methylation

Answer 22

Occur on lysine, influencing gene expression

Question 23

Ubiquitination

Answer 23

Attachment of ubiquitin to lysine residues, tagging proteins for degradation

Question 24

Primary structure (Protein)

Answer 24

The sequence of amino acids in a polypeptide chain

Question 25

Secondary structure (Protein)

Answer 25

Folded structures that form within a polypeptide

Question 26

α helix

Answer 26

The carbonyl (C=O) is hydrogen bonded to the amino H (N-H) of an amino acid that is four down the chain.

Question 27

β pleated

Answer 27

Polypeptide chain line up next to each other, forming a sheet-like structure held together by hydrogen bonds. (the R groups extend above and below the plane of the sheet)

Question 28

Tertiary structure (Protein)

Answer 28

The overall three-dimensional structure of a polypeptide, most proteins have.

Question 29

Disulfide bonds (safety pins)

Answer 29

Covalent linkages between the sulfur-containing side chains of cysteines

Question 30

Quaternary structure (Protien)

Answer 30

Subunits, protein consisting of more than one amino acid chain. DNA is composed of ten subunits

Question 31

Denatured proteins

Answer 31

Turn back into an unstructured string of amino acids

Question 32

Hydrophobic interactions

Answer 32

Non-polar amino acid side chains tend to cluster together inside the protein, release water, increasing the entropy of the system.

Question 33

Hydrogen bond

Answer 33

Form between polar side chains and contribute significantly to the protein's stability

Question 34

Ionic bonds (Salt bridges)

Answer 34

Form between positively charged (basic) and negatively charged (acidic) side chains

Question 35

Van der Waals forces

Answer 35

low fluidity of cell membranes

Question 36

Entropic (Randomness)

Answer 36

Protein folding is driven by a balance of enthalpic and entropic changes

Question 37

Conformational entropy

Answer 37

Decreases its conformational entropy/ offset by other entropic gains

Question 38

Solvent entropy

Answer 38

When hydrophobic chains cluster --> water being release --> increases the entropy of the surrounding water molecules

Question 39

Molecular Chaperones

Answer 39

Preventing improper interactions that can lead to aggregation or misfolding

Question 40

Chaperonins

Answer 40

Cylindrical complexes that provide a protected environment for protein folding