Types of proteins 3.7 Flashcards

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1
Q

what are the characteristics of globular proteins

A

globular proteins are compact, water soluble and usually roughly spherical in shape

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2
Q

how are globular proteins formed

A

they form when proteins fold into their tertiary structures in such a way that the hydrophobic R-groups on the amino acids are kept away from the aqueous environment.
The hydrophilic R-groups are on the outside of the protein.

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3
Q

how does the structure of globular proteins effect its properties

A

due to the proteins structure they are soluble in water as the hydrophilic R-groups are on the outside

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4
Q

what protein type is insulin and what is its function

A

insulin is a globular protein, it is a hormone involved in the regulation of blood glucose concentration, hormones are transported by blood and so need to be soluble
hormones also have to fit into specific receptors on cell-surface membranes to have their effect and therefore need to have precise shapes

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5
Q

what are conjugated proteins

A

conjugated proteins are globular proteins that contain a non-protein component called a prosthetic group

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6
Q

what are proteins with no prosthetic group called

A

simple proteins

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7
Q

what is an example of a prosthetic group else where in biology

A

haem groups are examples of a prosthetic group. they contain an iron (II) ion (Fe2+)
catalase and haemoglobin both contain haem groups

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8
Q

what is catalase and what is its function

A

catalase is an enzyme
catalase is a quaternary protein containing 4 haem prosthetic groups.
The presence of the iron II ions in the prosthetic groups allow catalase to interact with hydrogen peroxide and speed up its breakdown

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9
Q

what are fibrous proteins

A

fibrous proteins are formed from long, insoluble molecules

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10
Q

what is the structure of fibrous protein

A

-high proportion of amino acids with the hydrophobic R-groups in their primary structures
-They contain a limited range of amino acids, usually with small R-groups
-The amino acid sequence in the primary structure is usually quite repetitive

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11
Q

what are some examples of fibrous proteins

A

Keratin, elastin and collagen are examples of fibrous proteins

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12
Q

where is keratin found in the body

A

keratin is a group of fibrous proteins present in hair, skin and nails.

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13
Q

what is the structure of keratin

A

It has a large proportion of the sulphur-containing amino acid (cysteine).
This results in many strong disulphide bonds (disulphide bridges) forming strong, inflexible and insoluble materials.

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14
Q

what does the number of disulfide bonds influence about a compound and give an example where this can be seen

A

The degree of disulfide bonds determines the flexibility - hair contains fewer bonds making it more flexible than nails, which contain more bonds

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15
Q

where is elastin found in the body

A

elastin is a fibrous protein found in elastic fibres (along with small protein fibres)

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16
Q

where are elastic fibres found

A

elastic fibres are present in the walls of blood vessels and in the alveoli of the lungs

17
Q

what properties does elastic fibres give the structures its found in

A

they give these structures the flexibility to expand when needed, but also to return to their normal size

18
Q

what is the structure of elastin and how it is stabilised

A

elastin is made by linking many soluble tropoelastin protein molecules to make very large, insoluble and stable, cross-linked structure
The structure is stabilised by cross-linking covalent bonds involving the amino acid lysine, but the polypeptide structure still has flexibility

19
Q

what is collogen and where it is found

A

it is a connective tissue found in skin, tendons, ligaments and the nervous system
in some tissues multiple fibres of collagen aggregate into larger bundles. This is the structure found in ligaments and tendons. In skin, collagen fibres form a mesh that is resistant to tearing

20
Q

what is the structure of collagen

A

Collagen molecules have 3 polypeptide chains wound around each other in a triple helix structure to from a tough, rope-like protein
Many hydrogen bonds form between the polypeptide chains forming long quaternary proteins with staggered ends. These allow the proteins to join end to end, forming long fibrils called tropocollagen

21
Q

what is the function and features of tropoelastin

A

tropoelastin molecules are able to stretch and recoil without breaking, acting like small springs. They contain alternate hydrophobic and lysine-rich areas

22
Q

How is elastin formed

A

elastin is formed when multiple tropoelastin molecules aggregate via interactions between the hydrophobic areas.

23
Q

what is the function of elastin

A

elastin confers strength and elasticity to the skin and other tissues and organs in the body

24
Q

whats the structure of the polypeptide chains involved in the structure of collagen

A

Every 3rd amino acid in the polypeptide chains is glycine, which is a small amino acid. Its small side allows the 3 protein molecules to form a closely packed triple helix.

25
Q

How is collagen stabilised by its structure

A

collagen contains high proportions of the amino acid proline and hydroxyproline. The R-groups in these amino acids repel each other and this adds to the stability of collagen