Proteins 2 Flashcards

(28 cards)

1
Q

what are the general functions of proteins? (9)

A
  • movement
  • enzyme
  • structural
  • protection
  • storage
  • receptors
  • transport
  • hormones
  • control gene expression
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2
Q

what are glycoproteins?

A

compounds composed of protein and carbohydrate

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3
Q

how are glycoproteins formed?

A

through post translational modification (glycosylation)

- a sugar molecule attaches to an amino acid

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4
Q

give an example of an amino acid that attaches a sugar group to the - N (amine) group (i.e forms a glycoprotein)

A

asparagine

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5
Q

give an example of an amino acid that attaches a sugar group to a O atom (i.e forms a glycoprotein)

A

hydroxylysine, serine. threonine

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6
Q

give an example of a glycoprotein

A

immunoglobulin

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7
Q

where does glycosylation occur?

A

in the endoplasmic reticulum and golgi apparatus

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8
Q

what are the roles of glycoproteins? (5)

A
  • protein stability
  • increased solubility
  • protein orientation
  • cell signalling
  • cell recognition
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9
Q

what is HbA1C?

A

a type of glycoprotein (glucose attaching to red blood cells) that helps to show control of blood gluocse in diabetics over a longer period of time (2-3 months)

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10
Q

what are lipoproteins?

A

protein and lipid molecules that are joined either covalently or non-covalently

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11
Q

what is the function of lipoproteins?

A

transport water insoluble fats and cholesterol in the blood

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12
Q

give an example of a lipoprotein

A

HDL, LDL, Cryoglobulins

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13
Q

what is an LDL receptor?

A

a glycoprotein present on the surface of all body cells that binds to apoB on LDLs

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14
Q

what is the function of LDL receptors?

A

to bind to apoB on LDLs leading to the internalisation of LDL and its breakdown which signals the body to stop producing cholesterol

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15
Q

what is familial hypercholesterolemia?

A

an inheirited autosomnal dominant disorder in which faulty LDL receptors are produced

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16
Q

whata re the symptoms of FH?

A

often no symptoms are present and only blood tests highlight abnormal LDL levels. In some cases cholesterol is deposited in tendons, skin and arteries.

17
Q

what are metalloproteins?

A

a protein molecule with a bound metal ion

18
Q

what are the functions of metalloproteins?

A
  • enzymes
  • storage
  • signalling
  • transport
19
Q

what is the function of globular proteins?

A

have varied functions

- can act as hormones, enzymes or transporters

20
Q

what is the function of fibrous proteins?

A

are structural proteins e.g bone matrices, muscle fibre, connective tissue

21
Q

what is the structure of haemoglobin?

A

four polypeptides held toether in a quarternary structure with a haem group at the centre of each polypeptide

22
Q

what is co-operative binding?

A

a process in which oxygen binds to one subunit which alters the shape of the other subunits making it easier for more oxygen to bind

23
Q

what causes sickle cell anaemia?

A

a single base change which results in valine being coded for instead of glutmic acid
- valine is hydrophobic and glutamic acid is hydrophilic and so different interactions form

24
Q

what are the features of sickle cells?

A
  • have a crescent shape (sickle shape)
  • insoluble and at low concentrations of oxygen form crystals (leading to infarction)
  • give up oxygen to tissues more easily than normal red blood cells
25
what is the repeating subunit in collagen?
- (glycine - X - proline) - | * X is either alanine, hydroxyproline or lysine
26
how do collagen fibres form?
polypeptide coils to form a helix ---> 3 polypeptides then coil round each other (triple helix) ---> hydrogen bonds hold the helices together forming microfibrils which then form fibrils and then fibres
27
what causes scurvy?
lack of vitamin C - vitamin C needed to convert proline to hydroxyproline and lysine to hydroxylysine - both of these forms need to make hydrogen bonds and so lack of them forms weaker collagen fibres
28
what cause osteogenesis imperfecta (brittle bone disease)
glysine substituted for a larger amino acid which prevents the polypeptides from packing together to form tight helices and so weaker interactions form better fibres - secondary and tertiary structure lost