SfM - Proteins Flashcards

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1
Q

what is a protein?

A

macromolecule, made of amino acids, arranged in a particular structure to carry out a specific function

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2
Q

what do proteins do?

A

involved in biological processes
structural - actin=scaffold, keratin=skins
functional=enzymes/antibodies

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3
Q

how are amino acids made?

A

composed of either DNA or RNA nucleotides
DNA = a, c, g & t
RNA = a, c, g & uracil
Three nucleotides code for AAs

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4
Q

how many AAs are there in the body?

A

20

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5
Q

what is an amino acid composed of?

A

amine group and carboxylic acids. have a variable R group

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6
Q

are amino acids chiral?

A

yes, every aa except glycine has 4 different groups surrounding the carbon

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7
Q

are aa’s affected by pH?

A

low pH AA’s are cations (+)

high pH AA’s are anions (-)

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8
Q

what are aliphatic AA’s?

A

AA’s with hydrocarbon chain in R group

alanine, valine, iso/leucine

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9
Q

what are aromatic AA’s?

A

AA’s with benzene ring in R group

phenylalanine, tyrosine, tryptophan

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10
Q

sulphur-containing AA’s?

A

cysteine, methionine

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11
Q

basic AAs

A

long hydrocarbon chain that finishes in NH

arginine, lysine, histidine

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12
Q

acidic AAs

A

AAs have a C=O or C-O

aspartate, glutamate

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13
Q

polar AAs

A

AAs have carboxyl group in R group

serine, threonine, asparagine, glutamine

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14
Q

what is a proteins primary structure?

A

the sequence of AAs bonded in polypeptide chain

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15
Q

what is secondary structure?

A

the 3D spatial arrangement of AAs and their bonding (H-bond)
alpha helix
beta pleated sheet

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16
Q

what is the tertiary structure?

A

when functional groups (R chain) on AAs, interact with another - van der waals, ionic, hydrogen, disulphide, hydrophobic interactions
all functional proteins exist in this form

17
Q

what is the quaternary structure?

A

every polypeptides interact with one another

haemoglobin contains 4 tertiary polypep structures and 4 iron containing heme groups

18
Q

how does denaturation affect proteins?

A

chemical bonds in the protein are broken down - functionality is lost as it needs to be 3D (v.rare for denaturation to break primary structure)

19
Q

what are the main functions of proteins?

A

structural, enzymatic, contractile, defensive, storage, storage, receptors, hormonal, transport

20
Q

what is a glycoprotein?

A

proteins with 1 or more carbohydrates covalently attached

involved in stability, solubility, cell signalling

21
Q

what is a lipoprotein?

A

proteins combine with fat/lipids to form lipoproteins

found in cell membranes, transport hydrophobic molecules

22
Q

what is a metalloprotein?

A

protein molecules with a metal ion within their structures i.e haemoglobin
involved in enzymes, signal transduction, storage, transport

23
Q

in what form can proteins exist?

A

globular, fibrous and membranous

24
Q

globular proteins tend to be…

A

used in storage, hormones, transporters and structural

Myeloma is cancerous blood cells - globular proteins spill out

25
Q

fibrous proteins tend to be…

A

involved in muscle fibres and connective tissue

Scurvy - lack of vitamin C means collagen can’t be created

26
Q

membranous proteins tend to be…

A

membrane transporters, enzymes, cell adhesion molecules

Xanthelasma - LDL receptors not functioning or produced = lipid deposits under skin