B1.2 Protiens Flashcards

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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

A

20^x

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
Q

tertiary structure of a protein

A

polypeptide chain

26
Q

quaternary structure of a protein

A

assembled structures

27
Q

denaturations

A

when protiens start to break apart and become undone due to changes in temp and PH

28
Q

how can heat cause denaturations

A

causes vibrations between the molecule that can break intermolecular bonds or interactions

29
Q

examples of polypeptides

A

insulin
beta endorphin
alpha amylase
titin

30
Q

what does insulin bind to

A

Binds to insulin receptors (on liver, fat and muscle cells) causing absorption of glucose from the blood

31
Q

what is insulin composed off

A

Composed of 2 polypeptide chains as a short, globular protein