Biochemistry Flashcards

1
Q

What is the term for an aminoacid with a net neurtral charge?

A

Zwitterion

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What is term where the pH is at a range where the AA is a net charge of 0?

A

pI (isoelectric point)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is the precursor for catecholamines?

A

Tyrosine (more-polar aromatic AA)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What is the precursor for serotonin?

A

Tryptophan (more-polar, aromatic)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What amino acid serves as a methyl-group donor in methylation reactions?

A

Methionine (sulfur-containing)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What two amino acids are responsible for disulfide bonds?

A

Met and Cys

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What group of amino acids are hydrophilic, participate in hydrogen bond formations, and can be modified via phosphorylation and glycosylation?

A

Polar, uncharged amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What are the polar, uncharged amino acids?

A

Asparagine, Glutamine, Serine, and Threonine

asn, gln, ser, thr

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What are the aromatic amino acids?

A

Phenylalanine, Tyrosine, and Tryptophan

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What are the acidic amino acids?

A

Glutamate and Aspartate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What are the basic amino acids?

A

Arganine, Lysine, and Histidine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What are the nonpolar, aliphatic amino acids?

A

Glycine, Alanine, Proline, Valine, Leucine, and Isoleucine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What are the basic amino acids?

A

Arganine, Lysine, and Histidine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What are the essential amino acids?

A

His, Met, Threonine, Val, ILE, Phenylalanine, Tryptophan, Leucine, Lysine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What are the non-essential amino acids?

A

Alanine, Argasnine, Asparagine, Aspartate, Cysteine, Glutamate, Glutamine, Glycine, Proline, Serine, Tyrosine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What are the conditional essential amino acids and Why?

A

Glutamine and Arganine (trauma and child growth)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What are the main function of proteins?

A

Catalytic, Structure, Transport, Mobility, Immunity, and Communication

(STIM CC)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What is the name of the bond that links the N terminal and C terminal of amino acids?

A

Peptide bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

What is the primary protein structure?

A

The sequence of amino acids in a straight line

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

What is the secondary protein structure?

A

Alpha helices and beta sheet

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

How can a parallel and antiparallel B- pleated sheet be differentiated?

A

Parallel has both “sides” beginning and ending in N and C terminals respectively;

Antiparallel has N terminal (top) and C terminal (bottom) on the same side

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

What are the regular secondary protein structure patterns?

A

A-helix and B- pleated sheet

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

What are irregular secondary protein structure patterns?

A

Bends, loop,s and turns

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

What is the tertiary protein structure?

A

Multiple secondary units forming a 3D structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

What are structural domains?

A

Physically independent regions in the tert structure of a protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

What is the quaternary structure?

A

The associated of individual polypeptide chain subunits in a geometrically and stoichiometrically specific manner

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

What are the nonenzymatic denaturation of proteins?

A

Glycolysation, oxydation, nitrosylation, etc

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

What can denature a protein?

A

Very low/high pH and high temperatures

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

What class of enzymes catalyzes via redox reactions?

A

Oxidoreductases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

What enzyme class catalyzes the transfer of C-, N-, or P- groups

A

Transferases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

What enzymes catalyze the cleavage of bonds by addn of water

A

Hydrolases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

What enzymes catalyze cleavage of C-C, C-S, and certain C-N groups?

A

Lyases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

What enzymes catalyze rearrangement of optical or geometrical isomes?

A

Isomerases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

What enzymes catalyze formation of bonds between C, O, S, and N coupled to hydrolysis of high energy phosphates?

A

Ligases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

What are inorganic substances that are required for/increase the rate of catalysts?

A

Cofactors (Zinc, magnesium, iron II, iron III)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

What are organic molecules that are required to carry out catalysis?

A

Coenzymes (NAD, FAD, NADP, CoQ, CoA, etc)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

What term is used to quantify the measure of energy transfer between chemical reactions?

A

Gibbs Free Energy (G)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

What is the energy diff between reactants & a highly reactive intermediate that occurs during the formation of a product?

A

Energy barrier

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

Difference between the G of the reactants and the high energy intermediates.

A

Ea (activation energy)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

Human enzyme optimal temperature?

A

37 C

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

What temp do human enzymes begin to denature?

A

~40-42 C

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

What determines the optimal human enzyme pH?

A

Location

43
Q

What kinetic theory do enzymes typically follow?

A

Michaelis-Menten kinetics

44
Q

What assumptions are made with Michaelis-Menten kinectics?

A
  • [S] is far greater than [E]
  • [ES] does not change with time
  • No substantial back reaction from product to substrate
45
Q

What is Km in M-M kinetics?

A

the [S] needed to equal 1/2 Vmax

46
Q

What is the inhibition where an I is bound to the E via covalent bonds that cant be broken?

A

Irreversible Inhibition

47
Q

What is the type of reversible inhib where I binds to an allosteric site on E?

A

Noncompetitive

48
Q

What is the reversable Inhib where I competes with S to bind to the active site of E?

A

Competitive inhibition

49
Q

What is a primary property of lipids?

A

Soluble in organic solvents and hydrophobic

50
Q

What are the classification of lipids?

A

Glycerol and non-glycerol based

51
Q

What are some glycerol based lipids?

A

Simple: fats and oils

Complex: Phospholipids and Glycolipids

52
Q

What are some non-glycerol based lipids?

A

Steroids, Sphingolipids, and waxes

53
Q

What are the two ends called in a fatty acid?

A

Carboxylic end and Omega End

54
Q

What are the essential fatty acids?

A

Lineolic acid, alpha-lineolic acid

Human cells cant make cis-double bonds beyond 9 carbons

55
Q

Glycerol + Fatty Acid -3 H2O=

A

Triacylglycerol

56
Q

What are the functions of (glycero)phospholipids?

A

Strtuctural components of cell membrane, lipoproteins, pulmonary surfactant, bile, etc

Precursors for: PIP3 and 4, Diacylglycerol (DAG)

57
Q

What is the function of sphyngolipids?

A

Structural components of cell membranes and lipoproteins; Signaling precursors for secondary messengers

58
Q

What is the general composition of steroids?

A

Four fused rings arranged in a specific configuration (AKA ABCD ring system)

59
Q

What defines a sterol?

A

-OH group at position 3 of the A ring (cholesterol is an example)

60
Q

What are the functions of cholesterol?

A

1: Structural component of cell membranes (30%) and lipoproteins
2: precursor for synth of: Bile, bile acids, steroid hormones, Vit D

61
Q

What is mediator of the gene expression?

A

RNA

62
Q

What are the basic building blocks of nucleic acids?

A

Ribose sugar (5 carbon sugar), nitrogenous base, triphosphate good

63
Q

What are the five nitrogenous bases?

A

Adenine, Cytosine, Guanine, Thymine, Uracil

64
Q

Removing an OH group from a ribose sugar makes it more or less stable (deoxyribose)?

A

MORE stable

65
Q

What are the purines?

A

A,G (two rings, short name is bigger structure)

66
Q

Pyrimidines?

A

T, U, C (one ring)

67
Q

what is a nucleoside?

A

Ribose and nitrogenous base

68
Q

What is a nucleotide’s structure?

A

Ribose, base, triphosphate

69
Q

What bonds link nucleotides?

A

3’-5’ phosphodiester bonds (OH of C-3 of one sugar and OH of C-5 on the next one)

70
Q

How many NT pairs per DNA turn?

A

~10 pairs per 360 degree turn

71
Q

What direction do opposing DNA strands run?

A

Antiparallel

72
Q

What bonds connect opposing DNA strands?

A

Hydrogen bonds

73
Q

What are the three DNA forms? Right handed? Left handed?

A

B,A,Z DNA; B and A are right handed

74
Q

How many H-bonds are between A-T and C-G

A

2 and 3 respectively

75
Q

(A+G)=(C+T)

A

A%+T% and vice versa

76
Q

What can denature DNA?

A

Alkaline solutions and heat (break H bonds)

77
Q

What is the melting temperature of DNA (Tm) defined as?

A

When 50% of DNA is separated

78
Q

What relative conc of DNA nucleotides would “melt” first? A-T prominent (>60%) or G-C prominent?

A

DNA with more A-T bonds will “melt” faster since energy requirements to denature due to only two bonds is less

79
Q

What is a nucleosome?

A

~150 bp DNA wrapped around histone core proteins (8) and H1 linker histone

Contain Arganine and Lysine (basic charged that can bind to phosphate negative group backbone)

80
Q

What is the transcriptionally active segment of chromatin? Inactive?

A

Euchromatin; heterochromatin

81
Q

When is a chromosome visible?

A

Metaphase of mitosis/meiosis

82
Q

How do euchromatin and heterochromatin availability affect protein expression?

A

All cells have the same DNA, but different segments of that DNA is packed into heterochromatin depending on cell specialization (ie liver, kidney, etc)

83
Q

Is there a difference between stop codons of mitochondrial DNA and nuclear DNA?

A

Yes

84
Q

What is the structure of Mitochondrial DNA

A

Circular, double helix with 17 bp per turn

85
Q

What are RNA hairpins?

A

Self-bound double-stranded regions of RNA that form a loop

86
Q

What is the function of mRNA, tRNA, rRNA, miRNA?

A

m: carries genetic info from DNA to ribosomes
t: presents amino acids for synthesis on ribosomes
r: forms ribosomal subunits with ribosome
mi: not much known, various function

87
Q

What are the most diverse RNA types?

A

mRNA

88
Q

What is unusual about tRNA?

A

Has a high % of unusual bases (hydroxy-U, dihydro-U, etc)

89
Q

What is 80% of all RNA?

A

rRNA

90
Q

Where are haploid and diploid sets found?

A

Mature gametes and somatic cells respectively

91
Q

How many chromosomes in diploid? Haploid?

A

46 (2 pairs of 23) and 23 (no pairs)

92
Q

Where do single chromosomes in each pair come from?

A

Maternal and paternal DNA (via recombination)

93
Q

What are the protein coding sequences, introns or exons?

A

Exons, introns are excised

94
Q

How many genes are coded in DNA?

A

20-25,000 genes

95
Q

What two types of single copy genes exist?

A

Tissue-specific genes and housekeeping genes

96
Q

What are the DNA replication proteins?

A

DNA pol 3, DNA pol 1, Primase, DNA helicase, DNA ligase, Topoisomerase (prokaryotes)

97
Q

Which direction can DNA Pol add nucleotides?

A

5’-3’ direction (these are added nucleotides)

98
Q

What does topoisomerase do?

A

Removes supercoils in the helix by cleaving one or both DNA strands

99
Q

What is the DNA replication protein that some new anti-cancer drugs target?

A

Topoisomerase

100
Q

What does DNA polymerase do to prevent and correct mistakes in genetic code?

A

Proofreading and removal of incorrect nt (3’-5’ exonuclease activity)

101
Q

What is telomerase and how does it work?

A

Enzyme that has a short RNA molecule that acts as a reverse transcriptase that extends the short 3’ end formed via cell replication on the telomeres

102
Q

What cells are telomerase active in?

A

Stem cells and germ lines, not active in somatic cells

103
Q

How does telomerase activation in somatic cells present usually?

A

Cancer activates this, prevents rapid cell expansion aging

104
Q

Where are most reverse transcriptase enzymes found?

A

Retroviruses