Bio 33

Front 1

Central Dogma of gene expression

Back 1

DNA-->Transcription--> mRNA--> Translation--> Protein

Front 2

2 stages of protein synthesis

Back 2

1.Transcription (copying info)
2.Translation (changing)

Front 3

Transcription

Back 3

DNA-->mRNA
info in DNA (template strand) transcribed into mRNA by enzyme RNA polymerase

Front 4

Transcription Factos

Back 4

How a gene knows when to turn on/off
-Proteins taht bind DNA at specific sites
-Initiate transcription
-Bind to promoter region on DNA (start of gene)
-RNA polymerase binds to make mRNA

Front 5

Types of RNA

Back 5

mRNA= copy of gene, goes to ribosome
tRNA= carries amino acids to ribosomes (transfer)
rRNA= ribosomal RNA

Front 6

Steps of Transcription

Back 6

Initiation: binds transcription factors and RNA polymerase to promoter
Elongation: RNA polymerase adds nucleotides in 5'-3' direction
Termination: terminator sequence is reached

Front 7

RNA Processing

Back 7

Before leaving nucleus mRNA is processed
-5' cap
-3' poly A tail
-removal of introns(do not code for protein; cut out and coding regions spliced together)

Front 8

Translation

Back 8

mRNA--> Protein
Info in mRNA translated into protein
Ribosomes
Uses genetic code

Front 9

Genetic Code

Back 9

Triplet code (3mRNA bases=1 amino acid)
Non-overlapping
Redundant, more than 1 codon (3 base sequence) can specify an amino acid
Unambiguous, universal

Front 10

Steps of Translation

Back 10

Initiation: mRNA, small ribosomal unit, and tRNA come together
Elongation: large subunit attaches, tRNA molecules bring amino acide to ribosome
Termination: stop codon reached

Front 11

Protein synthesis

Back 11

Release factor binds to codon and terminates process

Front 12

How does tRNA know which amino acid to deliver?

Back 12

tRNA= anticodon complementary to codon on mRNA

Front 13

Protein structure

Back 13

4 levels (3D shape)
Protein function dependent upon proper structure
Change in structure leads to change in function

Front 14

Primary Structure

Back 14

the sequence of amino acids

Front 15

Secondary Structure

Back 15

folding into loops, coils, helices, sheets
Dependent on primary structure

Front 16

Tertiary Structure

Back 16

further folding as a result of interactions w/ water
Hydrophic regions repelled by water, will fold inward
Hydrophilic regions attracted to water, will fold outward

Front 17

Quarternary Structure

Back 17

Joining together of more than 1 polypeptide

Front 18

Protein folding

Back 18

Many molecules help to achieve 3D structure

Front 19

Chaperones

Back 19

Protein families that help proteins fold w/in cells.(protein export/import, assist correct folding, inhibit misformed proteins)

Front 20

Unfolded Protein response

Back 20

Slow/stop protein synthesis if not folding properly
Increased synthesis of chaperonins and other folding catalysts
Restoration of proper folding

Front 21

Proteasomes

Back 21

Protein tunnel that degrades misfolded proteins

Front 22

Protein misfolding--> disease

Back 22

Huntingtons Disease (protein huntington blocks proteasomes, leads to cell death)
Prion Disease (misfolded protein is infectious and causes other proteins to misfold)
Kuru Disase (human variant of prion diease, eat brain)
Chronic wasting in deer, elk