Biochemistry Flashcards

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1
Q

atoms with opposite charges attract (weak bond)

A

ionic bonds

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2
Q

bonds between atoms within same H2O molecule (strong bond)

A

covalent bonds

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3
Q

pair of electrons shared equally by two atoms

A

non polar covalent

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4
Q

pair of electrons shared unequally by two atoms

A

polar covalent

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5
Q

bond between 2 H2O molecules (weak bond)

A

hydrogen bonding

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6
Q

hydrogen bonding between water molecules, water is “sticky”, creates surface tension

A

cohesion

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7
Q

hydrogen bonding between water and other substances, meniscus

A

adhesion

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8
Q

movement of water through small tubes

A

capillary action

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9
Q

polarity makes H2O a good…

A

solvent

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10
Q

substance has an attraction to H2O

A

hydrophilic

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11
Q

substance doesn’t like H2O

A

hydrophobic

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12
Q

why is it important that ice floats?

A

surface ice insulates water below so life can survive in the winter

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13
Q

H2O resists changes in temperature

A

heat capacity

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14
Q

amount of heat absorbed to vaporize water at a constant temperature

A

heat of vaporization

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15
Q

on a pH scale 0-6 is…?

A

acidic

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16
Q

oh a pH scale 7 is…?

A

neutral

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17
Q

on a pH scale 8-14 is…?

A

basic

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18
Q

organic compounds with OH= alcohols, carbohydrates

A

hydroxyl

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19
Q

O double bonded to C, proteins

A

carbonyl

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20
Q

COOH, compounds w COOH= acids (amino and fatty acids), proteins

A

carboxyl

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21
Q

NH2, amines, NH2 acts as base, proteins

A

amino

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22
Q

S bonded to H, stabilizes proteins

A

sulfhydryl

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23
Q

P bonded to 4 O (PO4), connects C to and O, nucleic acids

A

phosphate

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24
Q

smaller organic molecules join together to form larger molecules

A

macromolecules

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25
Q

4 major classes of macromolecules

A

carbohydrates, lipids, proteins, nucleic acids

26
Q

combinations of C and H

A

hydrocarbons

27
Q

what properties do hydrocarbons have?

A

non polar and hydrophobic

28
Q

joins monomers by taking out H2O, monomer donates OH and other monomer donates H

A

dehydration synthesis

29
Q

uses H2O to breakdown polymers, opposite of dehydration synthesis, H2O is split into H and OH

A

hydrolysis

30
Q

if H+ = OH water is…

A

neutral

31
Q

if H+ > OH water is…

A

acidic

32
Q

study of carbon compounds

A

organic

33
Q

can contain hydrogen OR carbon, not both

A

inorganic

34
Q

carbon backbone

A

carbon skeleton

35
Q

what properties does oxygen have?

A

polar, hydrophilic

36
Q

bond that holds carbs together?

A

glycosidic

37
Q

bond that holds proteins together?

A

peptide

38
Q

bond that holds nucleotides together?

A

phosphodiester

39
Q

bond that holds lipids together?

A

ester

40
Q

unfolding of a protein?

A

denaturation

41
Q

conditions that disrupt denaturation?

A

temp, pH, salinity

42
Q

what structures does denaturation alter?

A

2, 3, 4

43
Q

name two nucleic acid polymers

A

DNA, RNA

44
Q

name two nucleotides

A

purines, pyrimidines

45
Q

double N ring base, adenine, guanine

A

purine

46
Q

single ring N base, cytosine, thymine, uracil

A

pyrimidines

47
Q

3 parts of a nucleotide?

A

nitrogen base (C-N ring), pentose sugar (5C) (DNA,RNA), phosphate group

48
Q

reducing the amount of energy to start a reaction

A

catalysts

49
Q

reactant which binds to enzyme

A

substrate

50
Q

end result of reaction

A

product

51
Q

enzymes catalytic site; substrate fits into this

A

active site

52
Q

enzyme theory? specific substrate fits into specific enzyme

A

lock and key

53
Q

enzyme theory? enzyme is slightly different than substrate but substrate comes in and changes its shape so they match up perfectly

A

induced fit

54
Q

type of activator? non protein and organic

A

coenzyme

55
Q

type of activator? non protein and inorganic

A

cofactor

56
Q

what factors affect enzymes?

A

enzyme concentration, substrate concentration,temp, pH and salinity

57
Q

type of inhibitor? inhibitor and substrate compete for active site

A

competitive inhibitor

58
Q

type of inhibitor? inhibitor binds to site other than active site

A

non competitive inhibitor

59
Q

type of inhibitor? changes shape of enzyme so it can’t bind to substrate

A

allosteric inhibitor

60
Q

type of inhibitor? inhibitor permanently binds to enzyme

A

irreversible inhibitor