Chapter 3 - Biological molecules - proteins Flashcards

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1
Q

what are peptides

A

polymers made up of amino acids - proteins consist of one or more polypeptides arranged as a complex macromolecule

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2
Q

what elements do proteins contain

A

Hydrogen Nitrogen Oxygen and Carbon

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3
Q

what is the basic structure of an amino acid

A

central carbon and hydrogen
left - amine group (NHH)
right - carboxyl group (COOH)
down - R group (different in all amino acids)

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4
Q

how do amino acids join to form peptides

A

condensation reaction between one amine group and one carboxyl group to form a peptide bond forming a dipeptide

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5
Q

what is the primary structure of a polypeptide

A

the sequence in which amino acids are joined (peptide bonds)

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6
Q

what are the two secondary structures

A

alpha helixes or beta pleated sheets (hydrogen bonds)

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7
Q

what are the interactions in the tertiary structure

A
between r groups:
hydrophobic/hydrophilic interactions (weak)
hydrogen bonds (weakest)
ionic bonds (strong)
disulphide bridges (strongest) - covalent bonds between r groups containing sulphur
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8
Q

describe a quaternary structure

A

interaction between two or more individual proteins called subunits (same bonds as in the tertiary structure)

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9
Q

describe the quaternary structure of haemoglobin

A

made of two sets of identical subunits - two alpha and two beta subunits; each subunit contains a prosthetic haem group

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10
Q

what is the test for proteins

A

biuret test - peptide bonds form violet coloured complexes with copper ions in alkaline solutions

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11
Q

what are the two main protein groups

A

globular and fibrous

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12
Q

what are the features of globular proteins

A

compact, water soluble and usually roughly spherical - hydrophobic r groups are on the inside and hydrophilic r groups are on the outside

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13
Q

what type of protein is insulin

A

globular

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14
Q

what is a conjugated protein

A

globular proteins containing a prosthetic group (non-protein component)

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15
Q

what is a simple protein

A

a protein without prosthetic groups

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16
Q

what does the haem in haemoglobin do

A

the iron in it can reversibly combine with oxygen - it allows it to carry oxygen in the blood

17
Q

what is the structure of catalase and what does it to

A

it is a quaternary protein containing four haem prosthetic groups. this allows catalase to breakdown hydrogen peroxide which is a by-product of metabolism

18
Q

what is a the structure of a fibrous protein

A

long insoluble molecule (due to hydrophobic r-groups)
limited range of amino acid, usually with short r-groups
repetitive structure

19
Q

give examples of fibrous proteins

A

keratin, elastin, collagen

20
Q

where is keratin found and what is its structure

A
hair, skin and nails
large proportion of sulphur containing amino acid - cysteine
many disulfide bridges
strong inflexible and insoluble
(hair contains less bonds)
21
Q

where is elastin found and what is its basic structure

A

in elastic fibres (walls of blood vessels and alveoli in lungs)
quaternary protein

22
Q

where is collagen found and what is its structure

A

connective tissue found in skin, tendons, ligaments and the nervous system
three polypeptides wound together in a long strong rope-like structure
has flexibility