T1 modules 3+4 Flashcards

1
Q

basic functions of proteins

A
  • transport + signalling (membrane pr-)
  • movement + structure (muscles)
  • enzymes
  • defense

*structural differences cause functional differences

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2
Q

where is genetic information stored in eukaryotes vs prokaryotes? describe structure and function of these organelles.

A

NOTE: chloroplasts and mitochondria store their own genetic info

EUKARYOTES (larger genome)
nucleus
- double membrane (nuclear enveloppe), contains chromosomes
- NUCLEOLUS contains ribosomal RNA
- NUCLEAR PORES connect nucleus to cytosol to export ribosomes m+rRNA, import nucleic acid building blocks + enzymes needed for transcription

PROKARYOTES (genome smaller)
nucleoid
- stores supercoiled DNA
- PLASMIDS: circular subunits that contain 1 or 2 genes. Can be transferred

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3
Q

structure and function of ribosomes

A

enzymes used to translate mRNA to proteins

in eukaryotes:
- components made in nucleus, transported to cytoplasm via nucelar pores
- FREE RIBOSOMES (soluble in cytoplasm)
- BOUND RIBOSOMES (can attach to endoplasmic reticulum)

in prokaryotes
- made in cytosol
- only free ribosomes

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4
Q

describe basic protein structure

A

AMINO ACIDS
- amino group, central C and H, carboxyl group and R side group

MONOMERS: single AAs
RESIDUES: name for linked AAs

POLYMERS/POLYPEPTIDES: strand of monomers bonded via condensation rxns between carboxyl and amino groups (peptide bond)

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5
Q

describe structures and process of protein folding

A

structures

PRIMARY: polypeptide strand
- peptide (covalent) bonds between amino and carboxyl
SECONDARY: polypeptide folding
- alpha helix (HB between carbonyl and carboxyl)
- beta pleated sheets (HB between carboxyl and amino)
- order of polypeptide responsible for this shape
TERTIATRY: 3D pr- shape
- R groups responsible for folding
QUATERENARY: multiple pr- come together
- e.g. hemoglobin

process

  • spontaneously
  • assisted folding via
    1) MOLECULAR CHAPERONES
  • bind to hydrophobic parts of pp chain to prevent incorrect folding
    2) CHAPERONINS
  • isolation chambers to prevent iterference
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6
Q

describe the journey of a protein after synthesis

A

if made in cytosol will stay in cytosol

if made by bound ribosomes…

1) PR- TO ROUGH ENDOPLASMIC RETICULUM
signal recognition particle (SRP) guides pp chain into ER. modified, then some stay, some leave
- SRP binds to signal sequence on pp chain, stops translation
- SRP binds to SRP receptor on ER membrane
- SRP receptor brings ribosome to a transmembrane channel, pr- synth starts again, chain threaded through channel

some pr- stay in ER, to vesicles that branch from ER and fuse with the golgi apparatus

MODIFICATIONS IN ER AND GA: GLYCOSILATION (+ carb chains for stability, folding and recognition)

2) GOLGI APPARATUS
- can stay in GA or tagged and shipped out via transport vesicles to specific destinations
- vesicle bilayer fuses with destination bilayer, releases soluble pr- and embeds transmembrane pr-
- can also be transported along microtubules - a component of the cells cytoskeleton that acts like a highway for pr- transport

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7
Q

transmembrane pores

A

AQUAPORINS
moves water
structure
- embedded in cell membrane
- hydrophobic exterior
- hydropphilic core

function:
- doesn’t change shape to move water. water bonds with hydrophilic groups inside and then displaces other water to move through

BACTERIAL PORIN
transmembrane pr in prokaryotes
- beta sheets form tube
- found in chloroplast + mitochondria = evidence for endosymbiotic theory of organelle evolution

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8
Q

how did we find out DNA was the heredity storage molecule

A

NEUFELD:
bacterial injection into mice
R strain: benign
S strain: virulent

THE GRIFFITH’S EXPERIMENT
living benign cells can get genetic info from dead virulent cells via TRANSFORMATION
- heated S strain to kill bacteria
- made samples with DNA, RNA, pr- removed
- added to R strain
- only samples with DNA present were lethal -> DNA molecule causing transformation

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9
Q

define transformation

A

“A change in cell behaviour resulting from the incorporation of genetic material from outside of the cell.

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10
Q

describe DNA structure

A

NUCLEOTIDE
- phosphate group, 5-C sugar, nitrogenous base, hydroxyl group

NITROGENOUS BASES
purines: single rings
- cytosine
- thymine
pyrimidines: double rings
- adenine
- guanine

ASSEMBLING A DNA MOLECULE
- condensation reaction (phosphodiester bond) between phosphate on 5’ C and hydroxyl on 3’C creates SUGAR PHOSPHATE BACKBONE

OVERALL STRUCTURE
- base pairs G+C (3HB), A+T (2HB)
- sides run antiparallel
- major and minor grooves-

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11
Q

types of RNA and their functions

A

mRNA: single stranded, translated to pr-
tRNA: never translated, carries AA to ribosomes during translation
rRNA: transcribed from ribosomal genes, perform translation

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12
Q

differences between DNA and RNA

A

STRUCTURE

DNA
- only 1 OH group on ribose sugar
- thymine
- T+A C+G

RNA
- 2 OH groups on ribose sugar
- uracil
- U+A C+G

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13
Q

how to tell if amino acids are hydrophilic or hydrophobic

A

philic
- able to make HB (will see NH2, OH)

phobic
- will see lots of carbons (like fatty acid chain, will be hydrophobic)
- benzene rings

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14
Q

name special amino acids

A

glycine, cystene and proline

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