Protein structure and function Flashcards

1
Q

Haemoglobin

A

Trasnports oxygen in blood

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2
Q

Alpha amylase

A

Breaks down starch within saliva

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3
Q

Collagen

A

Builds structures in mucsle and skin

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4
Q

Membrane bound ATP synthase

A

Lines inner membrane

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5
Q

DNA helicase & RNA polymerase

A

assist in transcription

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6
Q

trna

A

assist in translation

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7
Q

Amino acids components

A

Side chains dictate properties
Made of carbon, oxygen, hydrogen, nitrogen

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8
Q

Non polar amino acids

A

Hydrophobic properties

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9
Q

Polar amino acids

A

Hydrophilic properties

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10
Q

Primary protein structure

A

Sequence of amino acids - Polypeptide chain reading from N to C terminus

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11
Q

Residue

A

Monermic unit of polypeptide - Lyseine

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12
Q

Secondary structure

A

Amino acid sequence undergone localised folding held together by hydrogen bonds - Alpha and Beta

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13
Q

Alpha helix

A

Backbones form sprials with four amino acids per turn - Secondary structure

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14
Q

Beta sheets

A

One backbone faces one way, and u turns into opposite direction

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15
Q

Tertiary structure

A

Organised folding of protien with hydrophobic residues pointing inward and hydrophilic pointing out - Forms 3d structure of protien

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16
Q

Globular protiens structure

A

Tight, compact round blob

17
Q

Fibrous protiens structure

A

Long, elongated and spindly

18
Q

Quaternary structure

A

Mulitple polypeptide chains bonded together

19
Q

Inhibitors

A

Prevent susbtrate entering enymes active site

20
Q

Hydrogen bonds

A

Form backbone of protiens and folding
Weak bond but many

21
Q

Electrostatic interactions

A

Salt/ionic bridge between two oppositely charged groups

22
Q

Hydrophobic interaction

A

Clustering of polar and hydrophobic side chains away from water
weakest bond but most plentiful

23
Q

Covalent bond

A

Strongest bond that occyrs spontaneously in oxidising conditions - Disulphide bond

24
Q

Denaturation factors

A

ph
salt conc
temperature

25
Q

Heat denaturation

A

Health makes protiens insoluble making them unravel and lose shape or form random bonds

26
Q

Salt denaturation

A

Salt binding to a charged side chain can break electrostatic interactions