proteins Flashcards

(37 cards)

1
Q

what is a protein

A

macromolecule consisting of aminos acids arranged in a particular structure that enables it to carry out specific function

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2
Q

structural protein example

A

actin within a cell or keratin in skin

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3
Q

whats transcription

A

DNA—-> mRNA

-comes before translation

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4
Q

whats translation

A

mRNA—> protein synthesis

-mRNA used by cell as a code to make chains of AA’s that go onto form proteins

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5
Q

whats does uracil replace in mRNA

A

thymine

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6
Q

how many naturally occurring AA’s are there

A

20

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7
Q

describe an AA’s structure

A

amine group and carboxylic group and R group which is different each time

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8
Q

amine group

A

N-H2

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9
Q

what does chiral mean

A

its mirror image is not the same as itself

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10
Q

how are AA’s affected by a low Ph

A

carboxylic acid group takes up a hydrogen, and becomes slightly positive

the reverse is true at a high Ph

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11
Q

aliphatic amino acids

A

R group consisting of hydrocarbon chains

eg. glycine

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12
Q

aromatic amino acids

A

R group consisting of hydrocarbon ring

eg. phenylalanine

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13
Q

sulphur containing amino acids

A

contains a sulphur group

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14
Q

di-sulphide bridges

A

covalently bonded linkages that are contained between 2 sulphur containing AA’s and help increased strength

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15
Q

acid amino acids

A

eg. glutamate

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16
Q

basic amino acids

17
Q

polar amino acids

A

can carry a charge at the end of the R group

eg. serine

18
Q

miscellaneous amino acid

A

proline- has a unusual ring shape

19
Q

primary strcuture

A

sequence in which AA monomers are bonded together to form a polypeptide chain
-amino acid sequence

20
Q

peptide bond

21
Q

secondary struture

A

local interactions between stretches of a polypeptide chain

  • alpha helices
  • beta plated sheets
22
Q

tertiary structure

A

overall 3D arrangement when R groups of different amino acids interact

  • van der waals, ionic, hydrogen, disulphide bridges and hydrophobic interactions
  • functional proteins can’t exist without tertiary structure
23
Q

quaternary structure

A

more than one polypeptide chains join together

eg. HAEMOGLOBIN

24
Q

functions of proteins

A
enzymes
structural
receptors
hormones
transport
storage
defensive
contractile
25
conjugated proteins
protein to which another chemical group eg. carbohydrate is attached, by covalent bonding or other interactions
26
glycoproteins
proteins with 1 or more carbohydrate molecules covalently attached
27
ogliosaccharide
when a few carbohydrate monomers exist together in a chain, the carbohydrate is termed this
28
glycosylation
when carbohydrate molecules are attached to a protein
29
effects of glycosylation
stability solubility cell signalling orientation
30
lipoproteins
proteins that combine with lipids
31
functions of lipoproteins
found in cell membranes to transport hydrophobic molecules eg. cholesterol
32
apolipoprotiens
when lipoproteins form complexes with other lipoproteins transport fat around body, blood and CSF
33
metalloportines
protein molecules with a metal ions within their structures
34
example of metalloprotiens
haemoglobin
35
describe haemoglobin structure
- quaternary structure - 4 polypeptide chains- 2 alpha and 2 beta subunits - each subunit contains haem, and within each is 1 iron
36
what are the 3 categories proteins can be divided into functionally
globular fibrous membranous
37
globular proteins functions
``` storage enzymes hormones transporters structural ```