Proteins Flashcards

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1
Q

what are the monomers of proteins

and what are polypeptides

A

amino acids

more than two amino acids joined together

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2
Q

strucuture of amino acid

what elements are amino acids made up of

A

R
H2N–C – COOH
I
H

Carbon, Oxygen, Hydrogen and nitrogen

and sometimes sulfur

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3
Q

when peptide bonds are formed between amino acids what molecule is released

A

water (condensation)

HOWEVER the opposite of this reaction “hydrolysis” would add water to break the peptidde bond

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4
Q

how is a peptide bond formed

A

“OH” from COOH and “H” from H2N bond to form

C-N (peptide bond)

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5
Q

what are the four levels of a proteins structure

A

primary
secondary
tertiary
quaternary

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6
Q

what is the primary structure

A

the sequence of amino acids

a change in just one amino acid could change the entire strcuture of a protein

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7
Q

what is the secondary strucuture

A

hydrogen bonds form between amino acids in the polypeptide chain
making them COIL into an alpha helix or FOLD into a beta pleated sheet

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8
Q

what is the tertiary strucuture

A

the coiled or folded chain is often
COILED AND FOLDED FURTHER
more bonds form between different parts of the polypeptide chain

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9
Q

what is the quaternary structure

A

some proteins are made up of several polypeptide chains

the quaternary structure is the way these polypeptide chains are assembled together

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10
Q

what bonds hold the amino acids in the primary/secondary/tertiary structure together

A

primary- Peptide bonds
secondary- Hydrogen bonds
tertiary- affected by several bonds

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11
Q

what is an ionic bond in a protein

A

attraction between negatively and positively cahrged R groups

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12
Q

what is a disulfide bond

A

sulfur atom in one cystesine bonds to a sulfur atom in another cytesine forming a disulfide bond

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13
Q

Hydrophobic and hydrophillic interactions

A

when hydroPHOBIC R groups are close together in a protein they tend to clump together, which means that the hydroPHILLIC R groups are more likely to be pushed to the outside which affects the way the protein folds

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14
Q

Hydrogen bonds

A

weak bonds form between slightly positively charged hydrogen atoms in some R groups and slightly negatively charged atoms in other R groups

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15
Q

what are the four types of bonds that could be in the tertiary strucuture

A

ionic bonds
Disulfide bonds
hydrophobic/hydrophillic interactions
hydrogen bonds

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16
Q

what is a good feature of globular proteins

A

they are soluble so can be easily transported in fluids

17
Q

what is a conjugated protein

A

a protein group with a non protein group( prosthetic group) attached to it

the prosthetic group in haemoglobin is haem

18
Q

what is insulin
whats its function
what is one of its best features

what bond holds insulin molecule together

A

a hormone
regulate blood glucose levels.
Its soluble so can be transported in the blood

Disulfide bond

19
Q

Amylase

A

is am enzyme that catalyses the break down of starch

made up of a single chain of amino acids

20
Q

what is the secondary structure of Amylase made up of

A

BOTH alpha-helix and beta pleated sheets

21
Q

what are fibrous proteins

what are the three types of fibrous proteins

A

stuctural proteins

1) Collagen- found in animal connective tissue. Very strong
2) Keratin- found in skin,hairs,nails,feathers,horns. can be flexible as it is in skin or hard as it is in nails
3) Elastin- Found in elastic connective tissue, such as skin, large blood vessels and some ligaments. It is elastic so allows tissue to return to their original shape