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Central Dogma Flashcards

1
Q

central dogma

A

DNA -> RNA -> Protein
Process of building proteins from an instruction set

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2
Q

nucleic acid

A

a polymer made up of nucleotides

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3
Q

Polymer

A

a long molecule of small repeating units (monomers) bonded together

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4
Q

Nucleotide consistency (3)

A
  1. phosphate group
  2. 5-carbon sugar
  3. Nitrogenous base
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5
Q

DNA function

A

to store & transmit info in a sequence of bases attached to nucleotides

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6
Q

DNA Primary purpose

A

serves as template for synthesis

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7
Q

DNA secondary structure

A

-double helix
- strands are arranged in an antiparrallel way

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8
Q

Purine

A

Made of 9 atoms
-Adenine (A)
-Guanine (G)

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9
Q

Pyrimidine

A

Made of 6 atoms
-Cytosine (C)
-Thyamine (T- DNA only)
-Uracil (U- RNA only)

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10
Q

DNA molecule as a whole:

A

-hydrophilic
-stable: van der waals, hydrogen bonds

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11
Q

DNA Tertiary Stucture

A

Supercoils
-histones

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12
Q

RNA primary structure

A

(A,U,G,C)

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13
Q

RNA secondary structure

A

helical design
- hairpins

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14
Q

RNA tertiary structure

A

Folding

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15
Q

phosphodiester

A

bond forming the backbone of DNA/RNA, connects two monomers

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16
Q

hydrolosis

A

-opposite of condensation reaction
-uses water to break bonds
-breaks polymers into monomers

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17
Q

condensation reaction (dehydration synthesis)

A

-making monomers into polymers producing water

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18
Q

genetic code

A

sequence of info from bases

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19
Q

RNA unstability

A
  1. Catalyzes many chemical reactions.
  2. Contains genetic info
  3. Replication
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20
Q

Catalytic RNAs

A

ribozymes
-catalyze formation of peptide bonds when amino acids join to form polypeptides

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21
Q

Peptide

A

-bonds hold AAs together
- short chains of AAs
-long chain = polypeptide

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22
Q

Replication of RNA similarities to DNA

A

free nucleotides form H-bonds with complementary bases on template strand of RNA

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23
Q

replication of RNA differences to DNA

A

H-honds between this new double-stranded molecule must be broken “unzipped” by heat or enzyme

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24
Q

Steps of RNA replication

A
  1. complementary bases pair
  2. copied strand polymerizes
  3. copy and template separate
  4. copy serves as new template
  5. new copy polymerizes
  6. new copy is identical to OG
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25
Protein Structure
1. Primary: AA 2. Secondary: a-helices and B-pleated 3. Tertiary: 3D folding 4. Subunits (ex: hemoglobin)
26
PRoteins are made of ________________
amino acids
27
AA common structure
1. Hydrogen atom 2. Amino (NH2) functional group 3. Carboxyl (COOH) functional group (acidic) 4. Unique "R" group
28
R-group properties
-functional groups affect reactivity (ex: carboxyl, hydroxyl) -some AA have no functional groups and therefore rarely are in reactions
29
(R-group properties) Polarity and Charge affect ____________
solubility -polar R-groups are hydrophilic -non-polar R-groups are hydrophobic
30
Backbone: 1. R-group orientation
position of AA off backbone, whether it interacts with each other and water
31
Backbone: 2. Directionality
AA are written in order from N-terminus to C-terminus
32
N-terminus
free amino group (NH2)
33
C-terminus
has free carboxyl group (COOH)
34
Backbone: 3. Flexibility
single bonds on either side of peptide can rotate
35
Oligopeptide or peptide=
less than 50 AA
36
Polypeptide=
more than 50 AA
37
Primary protein structure
-unique sequence of AA -various lengths
38
Secondary protein structure:
-interactions between functional groups in peptide-bonded backbone within the same polypeptide chain -creates a-helices and B-pleated sheets
39
Tertiary protein structure
3D structure folding: - H-bonds - Hydrophobic interactions -Van Der Waals interactions - covalent & ionic bonds
40
Quaternary protein structure
combo of polypeptides ex: dimer, tetramer
41
vector
an organism that doesn't cause the disease itself but spreads infection
42
Mosquito (ectoparasites)
anopheles
43
Protist of malaria
plasmodium
44
hemoglobin
4 polypeptide subunits - a subunits are identical - B subunits are identical -each subunit binds to a non-protein group called a heme
45
Malaria is hard to control because
1. Difficult to develop a vaccine because it evolves quickly 2. Natural selection favors mosquito strains that are insecticide resistant
46
Change in AA to show sickle cell
Normal: (5, Pro)-(6, Glu)-(7,Glu) Sickle: (5, Pro)-(6, Val)-(7, Glu)
47
Heterozygote advantage for sickle
sickled RBCs are deoxygenated, and therefore a poor host for Plasmodium
48
What directs protein folding
the sequence of AA in primary structure of proteins
49
What controls the elements of protein function
folding of polypeptide chains
50
the combination of the 4 levels of protein structure
responsible for the diversity of sizes and shapes of proteins
51
denatured proteins
unfolded proteins, h-bonds and disulfide bonds are broken
52
heat shock proteins
-molecular chaperones -recognize denatured proteins by binding to hydrophobic patches
53
disordered proteins
regions that lack structure and are inactive
54
ordered proteins
active region with structure
55
Prions
-alternate forms of proteins found in healthy individuals -smallest known infectious particle -same AA sequence but protein shape is different -ex: mad cow disease
56
Genes
made of DNA and carry the instructions for making and maintaining on individual
57
gene expression
the process of converting stored info into functional molecules (proteins)
58
the genetic code hypothesis
-genes contain the info to specify the AA of one protein -the info encoded in the base sequence of DNA isn't directly translated into the amino acid sequence
59
mRNA
-short-lived -found to carry info from DNA to ribosome
60
enzyme ______________ is required to synthesize RNA
RNA polymerase
61
transcription
copying info (DNA --> mRNA)
62
translation
using info (mRNA --> proteins)
63
mechanism (proximate)
-gene/DNA sequence that's transcribed and translated into a protein -different amino acid
64
Adaptation (ultimate)
natural selection, sexual selection
65
Phylogeny (ultimate)
-close relatives
66
genetic code
the sequence of info presented in both nucleotides and AA
67
mRNA communcation
amino acids -> triplet code ->each amino acid is specified by a group of 3 bases (codon)
68
Start codon
methionine AUG
69
end codon
UAA, UAG, UGA
70
mRNA base #
1 -> 4 AA 2 -> 16 AA 3 -> 64 AA
71
our genetic code:
1. redundant almost all AA have 1+ codon 2. unambiguous a codon can code for one AA 3. non-overlapping each codon is read sequentially 4. nearly universal almost all species use these same AA 5. conservative if codons have same AA, the first 2 bases are the same
72
Point mutation:
a single base change
73
types of point mutation
1. Missense 2. Silent 3. nonsense 4. frameshift
74
Missense
causes codon to signal different DNA
75
silent
signals a different codon but doesn't change AA sequence
76
nonsense
change in a codon to a stop codon
77
frameshift
alters how codons are read
78
chromosome level mutations
changes to chromosome # or composition occurs in a cell
79
CLMs: Mistakes during meiosis or mitosis
movement of chromosomes into new cells or gametes
80
polypoidy
more than 2 copies of chromosomes
81
anenploidy
few or more copies dur to loss or addition of chromosomes
82
CLMs: breaks and/or reattachment
inversion (flipped)
83
translocation
when a segment breaks off & attaches to a new chromosome
84
duplication and deletion
additional copies of chromosomes chromosomes lost completely
85
four mechanisms that shift allele frequencies
1. Natural selection 2. genetic drift 3. gene flow 4. Mutation

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