GB1: Chapter 5B

Question 1

gene

Answer 1

amino acid sequence of polypeptide

Question 2

nucleic acid/polynucleotides

Answer 2

polymers of nucleotides

Question 3

Sugars in DNA/RNA

Answer 3

DNA: deoxyribose (lacks an oxygen at 2’C on ring)
RNA: ribose

Question 4

dehydration synthesis/condensation reaction

Answer 4

covalently bonding 2 monomers together with a byproduct of water

Question 5

hydrolysis

Answer 5

breaking covalent bond of polymer with input of water to create monomers

Question 6

enzymes

Answer 6

specialized macromolecules that speed up chemical reactions

Question 7

nitrogenous bases

Answer 7

adenine, guanine, cytosine, thymine (DNA), uracil (RNA)

Specific information carried in gene is encoded by specific sequences of nitrogenous bases

these determine amino acid sequence, as well as protein’s shape and function

Question 8

nucleotides

Answer 8

composed of phosphate group, pentose sugar (DNA: deoxyribose sugar, RNA: ribose sugar), nitrogenous base

Question 9

pyrimidine

Answer 9

1 six-sided ring of carbon and nitrogen atoms

cytosine, thymine, uracil

Question 10

purines

Answer 10

1 six-sided ring fused to five-sided ring

adenine, guanine

Question 11

Double helix

Answer 11

DNA has 2 strands of nucleic acids wound around an imaginary axis, held together by hydrogen bonds formed between paired nitrogenous bases

Question 12

antiparallel

Answer 12

2 sugar-phosphate backbones run in opposite 5’ to 3’ directions

Question 13

phosphodiester linkage

Answer 13

covalently bonds 2 nucleotides together through dehydration synthesis
[3’C OH group covalently bonded to phosphate’s H+ (that was attached to the OH group in water)]

Question 14

ester linkage

Answer 14

covalently bonds 2 triglyceride/fat molecules together through dehydration synthesis
(the H+ of the hydroxyl of glycerol molecule covalently bonds to OH of fatty acids)

Question 15

peptide bonds

Answer 15

covalently bonds 2 amino acids together through dehydration synthesis
[OH of C-terminus (carboxyl group) covalently bonds to H+ of N-terminus (amino group)]

Question 16

complementary base pairing (w/ H bonds)

Answer 16

A - T (DNA): 2 hydrogen bonds
G - C: 3 hydrogen bonds
A - U (RNA): 2 hydrogen bonds

complementary base pairing allows DNA to be replicated for cellular division

Question 17

RNA is special (with tRNA ex)

Answer 17

Single-stranded, so different RNA molecules can base pair, or even different regions on same RNA strand can. this allows for RNA to take on many shapes and thus have more functions

tRNA: there is complementary base pairing among nucleotides on tRNA that are antiparallel to each other

Question 18

proteins

Answer 18

folded polypeptide(s) with specific functional final 3D shape

Question 19

amino acids

Answer 19

monomer of proteins; organic molecule with amino group (n-terminus), carboxyl group (c-terminus), and r-group (side chain)

Question 20

R-group (side chain)

Answer 20

physical/chemical properties of side chain dictates unique attributes of amino acid, contributing to how polypeptide functions

Question 21

Types of R-groups

Answer 21

nonpolar - makes amino acid hydrophobic

polar: makes amino acid hydrophilic

charged: makes amino acid hydrophilic
+ = makes amino acid basic
- = makes amino acid acidic (usually acidic amino acids are - charged due to presence of carboxyl group that is usually dissociated at cellular pH)

Question 22

polypeptide

Answer 22

long strings of amino acids bonded together, NOT a protein

Question 23

structure of protein

Answer 23

primary
secondary
tertiary
quaternary

primary, secondary, and tertiary all occur simutaneously
quaternary only happens sometimes

Question 24

primary structure of protein

Answer 24

polypeptides

Question 25

secondary structure of protein

Answer 25

interactions between partial charges of amine (+) and carboxyl (-) groups forming hydrogen bonds in the backbone of polypeptide (not R-groups) alpha helix and beta pleated sheet

Question 26

alpha helix

Answer 26

delicate coil held together by hydrogen bonding between every 4th amino acid

Question 27

beta-pleated sheets

Answer 27

2 or more segments of polypeptide chain lying parallel connected by hydrogen bonds between parts of the segments

Question 28

tertiary structure of protein (3 types of interactions to make this)

Answer 28

gives overall shape of polypeptide due to interactions of side chains of amino acids, has to do with chemistry of R-group hydrophobic interactions ionic bonds hydrogen bonds disulfide bridges/sulfide bond

Question 29

hydrophobic interactions in tertiary structure of protein

Answer 29

nonpolar regions experience van der waals/attraction through hydrophobicity

Question 30

ionic bonds in tertiary structure of protein

Answer 30

can form between acidic and basic R-groups

Question 31

hydrogen bonds in tertiary structure of protein

Answer 31

polar R-groups create charges, creating hydrogen bonds

Question 32

disulfide bridge/sulfide bond in tertiary structure of protein

Answer 32

ONLY between 2 cysteine monomers that have sulfhydrl groups (-SH) - This keeps protein stable for longer

Question 33

3 other influencers for protein folding

Answer 33

pH, salt concentration, temperature

Question 34

function of carbohydrates

Answer 34

- breaks down sugar polymers into monomers to use as energy

Question 35

6 function of lipids

Answer 35

- fatty compounds that give cell membranes structure - filters what gets in/out - absorbs vitamins - makes hormones - stores energy - helps in cell communication

Question 36

2 functions of nucleic acids

Answer 36

- storage/expression of genetic information - genetic info can be passed down form one gen. to next

Question 37

8 functions of proteins

Answer 37

- enzymes: catalyze rxns - defense: protection against disease - storage: stores amini acids - transport: transports substances - hormones: coordination of organism's activities - receptor: response of cell to chemical stimuli - contractile: helps with movement - structural: provides structural support

Question 38

catalysts

Answer 38

chemical agents that selectively speed up chemical rxns but not consumed by rxn

Question 39

sickle-cell disease

Answer 39

inherited blood disorder caused by substitution of 1 amino acid for a normal one in primary structure of hemoglobin (protein that carries oxygen in red blood cells). these sickle-shaped cells impede blood flow

Question 40

denaturation

Answer 40

protein unravels and lose its original shape, biologically inactive

Question 41

Gene expression

Answer 41

DNA directs RNA synthesis, RNA directs protein synthesis