Proteins Flashcards

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1
Q

Dipeptide

A
  • two amino acids joined together by peptide bond
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2
Q

Peptide bond (3)

A
  • bond between two amino acids
  • between amino group and carboxyl group
  • formed through condensation/ dehydration reaction
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3
Q

Describe primary structure of protein

A
  • sequence showing a linear chain of amino acids

- maintained through peptide bonds

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4
Q

Secondary structure of protein

A
  • partially 3D structure maintained by hydrogen bonds
  • alpha helix
  • beta pleated
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5
Q

Tertiary structure

A
  • interactions between the R groups to create a 3D shape
  • hydrophobic interactions
  • disulphide bonds
  • iconic bonds
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6
Q

Quaternary structure and example

A
  • more than one tertiary structures fitted together
  • weak R group interactions
  • Van de Waal forces between sub units
  • eg Haemoglobin
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7
Q

Describe Haemoglobin

A
  • globular
  • 4 subunits
  • 2 beta chains, 2 alpha chains
  • 4 haem groups
  • transports oxygen in the blood; haem group contain iron binds to oxygen
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8
Q

Describe collagen

A
  • fibrous
  • connective tissues; skin, tendons, ligaments
  • mainly glycerin
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9
Q

What is the amino acid generalised structure?

A
  • central CH
  • Amino group- NH2
  • carboxyl group; COOH
  • R group
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10
Q

Insulin

A

Hormone that controls blood glucose concentration

Globular

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11
Q

How are proteins used in signalling

A

Hormones
Act as chemical messengers at receptors of cells

Enzymes
Change receptors

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12
Q

Keratin

A

Fibrous

Structural protein

Found in; hooves, hair, scales, nails

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13
Q

Pepsin and lipase

A

Hydrolytic digestive enzymes of the gut

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14
Q

Prosthetic groups

A

In conjugated proteins

Not an amino acid

Eg Haem group

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15
Q

Tripsin

A

Globular Protease

Breaks down proteins first in alimentary canal

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16
Q

Fibrinogen

A

Protective protein

Essential for blood clotting

17
Q

Prothrombin

A

Blood clotting

18
Q

Elastin

A

Structural component

Skin and coverings

19
Q

Describe fibrous proteins and examples

A

Insoluble in water

Usually structural components; rope like strong shape

Parallel polypeptide chains held with cross links

Eg Collagen, silk, Heratin, fibrinogen

20
Q

Describe globular proteins and examples

A

Hydrophilic outside with hydrophobic inside

Eg Tripsin, Haemoglobin, DNA polymerase

21
Q

Biological functions of proteins. (6)

A
  • Enzymes: eg hydrolysed like amylase, protease and lipase in digestion.
  • Hormones: eg insulin which regulates blood glucose concentration
  • Contractile proteins: contract/ lengthen to enable movement eg actin and myosin in muscles.
  • Transport: Bind to and release substances. Eg haemoglobin for oxygen transport in blood.
  • Protective/ immune defence: Primary defends such as blood clotting factors with fibrinogen and thrombin. Antibodies which neutralise antigens.
  • Buffers: Amino acids and proteins are able to reduce pH. Haemoglobin can be reduced.