B1.2 Protiens Flashcards

1
Q

what are Proteins

A

Proteins are polymers (and macromolecules) made of monomers called amino acids

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2
Q

what determines a Proteins shape and therefore its function

A

The sequence, type and number of the amino acids within a protein

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3
Q

why are Proteins extremely important in cells and examples of protiens

A

all of the reactions necessary for life are dependent on the function of proteins

  • Enzymes
  • Cell membrane proteins (e.g. carrier)
  • Hormones
  • Transport proteins (e.g. haemoglobin)
  • Structural proteins (e.g. keratin, collagen)
  • Contractile proteins (e.g. myosin)
    oteins
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4
Q

what are Amino acids

A

monomers of polypeptides

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5
Q

how many amino acids found in polypeptides common to all living organisms

A

There are 20 amino acids found in polypeptides common to all living organisms

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6
Q

The general structure of all amino acids

A

central carbon atom, the alpha carbon, bonded to:

An amine/amino group -NH2
A carboxylic acid/carboxyl group -COOH
A hydrogen atom
R group

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7
Q

what is the r group

A

a side chain specific to each amino acid that gives particular chemical properties to that amino acid

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8
Q

how is a Peptide bond formed

A

condensation reaction of 2 amino acids resulting in the production of H2O

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9
Q

what is a condensation reaction

A

when two aminos combine to produce water

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10
Q

Dipeptides

A

formed by the condensation of two amino acids

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11
Q

alpha carbon

A

connects amine groups with carboxylic group as well as R group and a hydrogen

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12
Q

polar amino

A

polar if there is either an OH or NH in the R chain

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13
Q

non polar amino acid

A

No OH or NH in the r chain

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14
Q

essential amino

A

an amino acid that our body can’t produce so we need to consume

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15
Q

non essential

A

what our body produces and doesn’t need to consume

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16
Q

how to calculate amino acids

17
Q

oligopeptide

A

2-20 amino acids

18
Q

polypeptide

A

more than 10 amino acids

19
Q

tripeptide

A

condensation reaction between dipeptide and amino acids results in tripeptide

peptides of three amino acid residues

20
Q

peptide linkage

A

a covalent bonding of the amino group of one amino acid to one of the carboxyl group of another

21
Q

Role of proteins

A

versatile

some examples -
Speeding up cellular reactions
blood clotting
cell adhesion
hormones
cell receptions

22
Q

what is insulin

A

A hormone produced and secreted by cells in the pancreas

23
Q

primary structure of a protein

A

chains of amino acid

24
Q

secondary structure of a protein

A

helix formed by amino chains

25
tertiary structure of a protein
polypeptide chain
26
quaternary structure of a protein
assembled structures
27
denaturations
when protiens start to break apart and become undone due to changes in temp and PH
28
how can heat cause denaturations
causes vibrations between the molecule that can break intermolecular bonds or interactions
29
examples of polypeptides
insulin beta endorphin alpha amylase titin
30
what does insulin bind to
Binds to insulin receptors (on liver, fat and muscle cells) causing absorption of glucose from the blood
31
what is insulin composed off
Composed of 2 polypeptide chains as a short, globular protein