Protein levels of structure Flashcards

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1
Q

what are the 4 different heirachal structures for proteins

A

primary, secondary, tertiary and quaternary

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2
Q

primary structure

A

the linear seuqnece/order of amino acid in a polypeptide chain(s), they are often written as 3 letter acid codes with hyphens representing the peptide bonds

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3
Q

what does primary structure determine

A

as the order of aamino acids is unique to each protein it determines its function becuase it can then fold to form additinal structures

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4
Q

what is secondary structure

A

decribes the 3 dimensional form of local segments of a polypeptide chain, it is the result of the interactions between nearby amino acids

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5
Q

two examples of secondary structure

A

alpha helix and beta pleated sheets

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6
Q

examples of interactions between amino acids that cause secondary structure

A

negative r groups and positive r groups attract and polar r groups attract, pulling them closer to each other

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7
Q

what does polar mean, how is it shooown

A

when two elements are held by a covalent bond bond and the electrons arent shared evenly, e.g element is on a weird angle attached to another

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8
Q

what is an alpha helix

A

the right hand spiralling of the polypeptide, with the side chain pointing outwards, spiralling is caused by the repulsion between equally charged side chains

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9
Q

structure of alpha helix

A

is is held in a tight coil by the hydrogen bonds that form between the hydrogen from one amino acid and oxygen from four amino acids earlier

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10
Q

what does the alpha helix allow

A

the protein to stretch and then recoil and give a protein strength (e.g. keratin)

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11
Q

what is the strcture of the beta pleated sheets

A

when two or more lengths of a polypeptide run paralell/antiparallel and are held together by the hydrogen bonds between non-adjacent regions of the polypeptide

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12
Q

what do beta pleated sheets cause

A

for the protein to become more stretched and rigid the sheets make up fibroin (silk)

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13
Q

what is tertiary structure

A

the overall three dimensional shape of the protein, the shpe of the outer surface of the protein that is presented to other molecules

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14
Q

why does tertiary structure matter

A

the outer shape of a protein determines its function; biomacromolecules interact with each other mostly due to complementary shaoes and charrges

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15
Q

what rpoetins have quaternary structure

A

those with more than one polypeptide chain, results in globular or fibrous protein

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16
Q

what is quaternary structure

A

the assmeblly or cluster of sereval protein chains joined together to form a functional protein

17
Q

what is the difference between a protein and a polypeptide

A

a protein describes the function of something, something is a protein because it has a function. polypeptide is a structural word and describes a chain of amino acid monomers

18
Q

what is a conjugated protein

A

when a protein hav=s non-amino acid groups (prosthetics) attached to them

19
Q

how does a prosthetic influence the name of a protein

A

it is added to the start of the name of the protein e.g an added lipid - lipoprotein, carbohydrate group - glycoprotein

20
Q

what is a prosthetic group

A

a non-amino acid component bound tightly to a functional protein