proteins Flashcards

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

A

eg. lysine

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

A

c=O, NH2

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
Q

conjugated proteins

A

protein to which another chemical group eg. carbohydrate is attached, by covalent bonding or other interactions

26
Q

glycoproteins

A

proteins with 1 or more carbohydrate molecules covalently attached

27
Q

ogliosaccharide

A

when a few carbohydrate monomers exist together in a chain, the carbohydrate is termed this

28
Q

glycosylation

A

when carbohydrate molecules are attached to a protein

29
Q

effects of glycosylation

A

stability
solubility
cell signalling
orientation

30
Q

lipoproteins

A

proteins that combine with lipids

31
Q

functions of lipoproteins

A

found in cell membranes to transport hydrophobic molecules eg. cholesterol

32
Q

apolipoprotiens

A

when lipoproteins form complexes with other lipoproteins

transport fat around body, blood and CSF

33
Q

metalloportines

A

protein molecules with a metal ions within their structures

34
Q

example of metalloprotiens

A

haemoglobin

35
Q

describe haemoglobin structure

A
  • quaternary structure
  • 4 polypeptide chains- 2 alpha and 2 beta subunits
  • each subunit contains haem, and within each is 1 iron
36
Q

what are the 3 categories proteins can be divided into functionally

A

globular
fibrous
membranous

37
Q

globular proteins functions

A
storage
enzymes
hormones
transporters
structural