Biochemistry Flashcards

1
Q

AA structure includes

A

basic amino group, acidic carbonyl group, R group, H atom

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2
Q

L-AA are used to

A

synthesize proteins

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3
Q

AA under low pH conditions =

A

protonated

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4
Q

AA under high pH conditions

A

deprotonated

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5
Q

_ AAs can destabilize or break down alpha helical 2 structures

A

glycine and proline

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6
Q

proline does NOT contain an

A

aromatic ring

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7
Q

_ AAs are the target of phosphorylation b/c they contain a hydroxyl functional group

A

serine, threonine, and tyrosine

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8
Q

_ AAs can form salt bridges

A

basic & acidic

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9
Q

_ can be used to break disulfide bonds in a western blot

A

BME

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10
Q

peptide bond

A

dehydration reaction in which the amino group of 1 AA acts as a nucleophile and attacks the carboxyl group of another AA, releasing a water molecule

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11
Q

amino and carboxyl functional group form a

A

amide group

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12
Q

formation of a peptide bond is a _ reaction

A

endergonic (E from ATP)

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13
Q

_ bonds stabilize secondary structure

A

H

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14
Q

_ structure forms optimal conformation of a protein

A

tertiary

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15
Q

what are the different forces stabilizing peptide bonds?

A

H bonds, ionic bonding/salt bridges, D-D interactions, LDF, and disulfide linkages

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16
Q

proteins fold into a state that _ the entropy of the system

A

maximizes, but minimizes their own energy

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17
Q

causes of protein denaturation

A

temperature, salinity, pH

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18
Q

solvation layer

A

water molecules that surround a protein

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19
Q

isoelectric focusing

A

each protein migrates until its reaches its pI

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20
Q

pH < pI =

A

+ charged

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21
Q

pH > pI =

A
  • charged
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22
Q

native PAGE

A

separates proteins in their native tertiary state based on size and charge

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23
Q

SDS PAGE

A

separates proteins only based on their molecular mass NOT charge

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24
Q

western blot

A

proteins are visualized on a gel to see if a particular protein is present

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25
Q

formation of ES complex _ activation energy

A

lowers

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26
Q

oxidoreductase

A

transfer of electrons which result in change in oxidation state

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27
Q

transferase

A

transfer of a functional group from 1 molecular to another

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28
Q

hydrolase

A

breakdown of a covalent bond using water

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29
Q

lyase

A

breakdown of a covalent bond without water or electron transfer (oxidation)

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30
Q

isomerase

A

rearrangement of bonds within a molecule

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31
Q

ligase

A

formation of a covalent bond between 2 large molecules

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32
Q

enzyme approximation

A

enzyme catalyzes the reaction by bringing reactants in close proximity

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33
Q

covalent catalysis

A

enzyme catalyzes the reaction by forming a temporary covalent bond with the reactant

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34
Q

acid-base catalysis

A

enzyme catalyzes the reaction by acting as a n acid/base

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35
Q

metal ion catalysis

A

enzyme catalyses the reaction by assisting in electrophilic or nucleophilic interactions/binds to substrate

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36
Q

cofactors

A

inorganic ions (like iron or magnesium) that aids in activity

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37
Q

coenzymes

A

organic helpers and vitamins that aid in activity

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38
Q

2 ways to affect enzyme kinetics

A

increasing substrate concentration, increasing enzyme concentration

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39
Q

increasing substrate concentration beyond vmax effect:

A

none since the enzyme’s AS is already saturated

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40
Q

competitive inhibition

A

bind to AS, Km increased Vmax no change

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41
Q

non-competitive inhibition

A

bind to enzyme at allosteric site, no change in Km, decrease in Vmax`

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42
Q

mixed inhibition

A

bind to enzyme or allosteric site, decrease in Vmax, increase/decrease in Km

43
Q

uncompetitive inhibition

A

bind to ES complex, both Vmax and Km decrease

44
Q

3 components of nucleotides

A

nitrogenous base, pentose sugar, and phosphate group

45
Q

4 nitrogenous bases

A

adenine, guanine, cytosine, thymine

46
Q

phosphodiester linkages

A

formed between the 3’ carbon of 1 sugar and the 5’ carbon of another

47
Q

nucleoside

A

pentose sugar attached to a nitrogenous base

48
Q

watson-crick & DNA

A

DNA is a double helix and strands lie anti-parallel to one another

49
Q

chargaff’s rule

A

total number of purines = total number of pyrimidines

50
Q

G-C have a higher melting point b/c

A

they have more H bonds

51
Q

hybridization of DNA

A

ssDNA can bind to another ssDNA of different origin if they have sufficient complementarity or base pairing

52
Q

role of water

A

capable of H bonding (F, O, N) = elevated BP

53
Q

lipid solubility

A

low solubility in water, high solubility in nonpolar organic solves (NP & hydrophobic)

54
Q

role of lipids

A

energy storage, cellular organization and structure, precursor molecule for vitamins and hormones

55
Q

fatty acids

A

building blocks of complex lipids which have a long C chain and carboxylic acid (most energy stroage)

56
Q

triacylglycerols (triglycerides)

A

3c backbone (glycerol) and 3 FA chains, store E and provide insulation

57
Q

phospholipids

A

have phosphate that replaces 1 of the FA, amphiphatic

58
Q

glycolipids

A

carbohydrate replaces the phosphate in phospholipids, found in myelinated membranes

59
Q

sphingolipids

A

have amino acid backbone` rather than glycerol found in triglycerides, have phosphate head and FA chain

60
Q

steroids

A

4-ringed structure which contains cholesterol, important for membrane fluidity and precursor to steroid hormones

61
Q

terpenes

A

pigments in the body (ex. vitamin A)

62
Q

waxes

A

formed by ester linkage between alcohol chain and long-chain FA

63
Q

eicosanoids

A

include prostaglandins, thromoxanes, etc Help to regulate BP, body temp, and muscle contraction

64
Q

what allows lipids to be transported into the blood?

A

lipoprotein!

65
Q

carbohydrates

A

have C-H bonds and alcohol chains, less E storage than lipids. join together via dehydration reactions

66
Q

topoisomerase

A

works at the region ahead o the replication fork to prevent supercoiling by introducing breaks in the DNA and then resealing them

67
Q

DNApol3

A

extends the primers, adds nucleotides in the 5’ to 3’ direction

68
Q

DNApol1

A

replaces the primers with new DNA

69
Q

DNApolII

A

has DNA proofreading ability and serves a repair fucntion

70
Q

telomerase

A

not usually active in somatic cells, but is active in germ cells

71
Q

mismatch repair

A

correct small insertions and deletions as well as correcting errors that occur right after replication is completed

72
Q

glycosylases

A

detects and removes a specific kind of damaged base

73
Q

2 pathways involved in double-stranded break repair

A
  1. Non-homologous end joining: two broken ends of the chromosomes are glued back together
    Introduces a small mutation
  2. Homologous recombination: information from the homologous chromosomes that matches the damaged one is used to repair the break
74
Q

amber codon

A

mutation occurs and causes an early stop codon in an mRNA sequence

75
Q

degenerate genetic code means

A

many AA are encoded by a few different codons

76
Q

missense codons

A

encode an incorrect AA

77
Q

nonsense coons

A

encode a premature stop codon

78
Q

Aminoacyl tRNA synthetases:

A

enzymes that load individual amino acids onto the tRNA

79
Q

eukaryotic transcription occurs in the

A

nucleus

80
Q

prokaryotic. transcription occurs in the

A

cytoplasm

81
Q

eukaryotes require _ to first bind to the promoter region

A

transcription facotrs

82
Q

RNA pol1

A

synthesizes rRNA

83
Q

RNApol2

A

located in the nucleus and syntehsizes all protein coding nucleuar premRNAs

84
Q

RNApol3

A

in nucleus, transcribes a variety of structural RNAs

85
Q

prokaryotes have 2 types of termination signals

A

Rho-dependent termination (protein dependent) and Rho-independent termination which is controlled by specific DNA sequences)

86
Q

small ribosome subunit

A

binding of the mRNA template

87
Q

large ribosome subunit

A

binds tRNAs (have A, P, and E sites)

88
Q

most post-translational mods happen in the

A

ER and Golgi

-ex: glycosylation, lipidation, ubiquitination, phosphorylation

89
Q

only AA that can undergo phosphorylation are

A

serine, tyrosine, and threonine

90
Q

euchromatic

A

part of coding regions

91
Q

heterochromatic

A

highly condensed, no coding, have regions that are silenced or suppressed by DNA mehtylation

92
Q

monocistrionic expression

A

a single DNA promoter directs the synthesis of an mRNA containing 1 gene (seen in eukaryotic mRNA)

93
Q

repressible operons

A

as long as the product of the pathway continues to be required by the cell, a repressible operon will continue to be expressed

94
Q

inducible operons

A

expression of this (lac) is typically induced only in the presence of the substrate

95
Q

lac operon

A

subject to activation in the absence of glucose, lactose must be present

96
Q

CAP

A

protein that binds to the promoters of operons that control in the processing of alternative sugars

97
Q

corepressor

A

protein that decreases gene expression by binding to a transcription factor that contains a DNA-binding domain
-Needs to recruit histone deacetylase which catalyzes the removal of acetal groups from lysine residues which makes the DNA less accessible to transcription

98
Q

oncogenes

A

cause cancer

99
Q

tumor suppressor genes

A

active in normal cells to prevent uncontrolled cell growth

Ex: p53: functions as a tsg and transcription factor

100
Q

proto-oncogenes

A

positive cell-cycle regulators, when mutated can become oncogenes and cause cancer

101
Q

acetylation

A

increases gene epxression

102
Q

Cpg islands

A

stretches of DNA with a high frequency of C and G pairs found in the promoter regions of genes, can be methylated

103
Q

what are the non-coding RNA

A

mi-RNA, snRNA, rRNA, tRNA

104
Q

mi-RNA

A

involved in post-transcriptional regulation of gene expression and silencing of RNA, suppress translation