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GB1 > GB1: Chapter 5B > Flashcards

GB1: Chapter 5B Flashcards

1
Q

gene

A

amino acid sequence of polypeptide

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2
Q

nucleic acid/polynucleotides

A

polymers of nucleotides

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3
Q

Sugars in DNA/RNA

A

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

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4
Q

dehydration synthesis/condensation reaction

A

covalently bonding 2 monomers together with a byproduct of water

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5
Q

hydrolysis

A

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

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6
Q

enzymes

A

specialized macromolecules that speed up chemical reactions

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7
Q

nitrogenous bases

A

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

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8
Q

nucleotides

A

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

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9
Q

pyrimidine

A

1 six-sided ring of carbon and nitrogen atoms

cytosine, thymine, uracil

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10
Q

purines

A

1 six-sided ring fused to five-sided ring

adenine, guanine

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11
Q

Double helix

A

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

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12
Q

antiparallel

A

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

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13
Q

phosphodiester linkage

A

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)]

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14
Q

ester linkage

A

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)

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15
Q

peptide bonds

A

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

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16
Q

complementary base pairing (w/ H bonds)

A

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

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17
Q

RNA is special (with tRNA ex)

A

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

18
Q

proteins

A

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

19
Q

amino acids

A

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

20
Q

R-group (side chain)

A

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

21
Q

Types of R-groups

A

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)

22
Q

polypeptide

A

long strings of amino acids bonded together, NOT a protein

23
Q

structure of protein

A

primary
secondary
tertiary
quaternary

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

24
Q

primary structure of protein

A

polypeptides

25
Q

secondary structure of protein

A

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

26
Q

alpha helix

A

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

27
Q

beta-pleated sheets

A

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

28
Q

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

A

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

29
Q

hydrophobic interactions in tertiary structure of protein

A

nonpolar regions experience van der waals/attraction through hydrophobicity

30
Q

ionic bonds in tertiary structure of protein

A

can form between acidic and basic R-groups

31
Q

hydrogen bonds in tertiary structure of protein

A

polar R-groups create charges, creating hydrogen bonds

32
Q

disulfide bridge/sulfide bond in tertiary structure of protein

A

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

33
Q

3 other influencers for protein folding

A

pH, salt concentration, temperature

34
Q

function of carbohydrates

A
  • breaks down sugar polymers into monomers to use as energy
35
Q

6 function of lipids

A
  • fatty compounds that give cell membranes structure
  • filters what gets in/out
  • absorbs vitamins
  • makes hormones
  • stores energy
  • helps in cell communication
36
Q

2 functions of nucleic acids

A
  • storage/expression of genetic information
  • genetic info can be passed down form one gen. to next
37
Q

8 functions of proteins

A
  • 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
38
Q

catalysts

A

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

39
Q

sickle-cell disease

A

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

40
Q

denaturation

A

protein unravels and lose its original shape, biologically inactive

41
Q

Gene expression

A

DNA directs RNA synthesis, RNA directs protein synthesis

GB1 (11 decks)

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