proteins, enzymes and ATP Flashcards

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1
Q

what three groups make up an amino acid

A

amino group
r group
carboxylic acid group

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2
Q

what is the amino group

A

H-N-H

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3
Q

what is the carboxylic acid group

A

OH-C–O

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4
Q

how many naturally occuring amino acids exist

A

20

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5
Q

what type of reaction occurs when two amino acids form a dipeptide

A

condensation reaction

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6
Q

what are the four levels of structure in protiens

A
  • primary
  • secondary
  • tertiary
  • quaternary-
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7
Q

what are the the bonds in proteins

A
  • hydrogen bonds
  • hydrophillic / phobic interactions
  • ionic bonds
  • disulfide bonds
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8
Q

what secondary structures of protein are there

A
  • alpha helix
  • beta pleated sheets
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9
Q

What is the difference between tertiary and quaternary structures

A

quaternary has two or more chains of polypeptides interlinked with eachother

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10
Q

what are polar molecules

A

partial negatives and partial positives charge on the two atoms

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11
Q

describe how peptide bond is formed between two amino acids to form a dipeptide

A

a condensation reaction occurs between the amino group and the carboxylic acid group

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12
Q

the secondary structure of a polypeptide is produced by bonds between amino acids - describe how

A

hydrogen bonds forming forming beta - sheets and alpha - helix

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13
Q

what type of proteins are enzymes

A

globular proteins

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14
Q

what do enzymes do

A

speed up rate of reaction
lowers activation energy without being used up

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15
Q

what is the lock and key model

A

substrate fit exactly into the shape of the enzyme

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16
Q

what is the induced fit model

A

enzyme changes the shape of its active site according to the shape of the substrate

17
Q

describe how the monomers join to form the primary structure of a protein

A

monomers join together in a condensation reaction to form a peptide bond. Process repeats and creates a sequence of amino acids

18
Q

what is the effect of PH on enzyme reaction

A

acid has H+ ions and alkali has OH- ions
interact with protein structure and alters ionic and hydrogen bonds
tertiary structure changes therefore active site changes and substrate no longer fits

19
Q

what is a competitive inhibitors

A

binds to enzyme active site
similar structure to substrate
slows production
mostly reversible

20
Q

what is a non competitive inhibitor

A

binds to the allosteric site on enzyme
alters the shape of the active site so substrate can no longer fit
slows production

21
Q

what is the use of ATP

A

when broken down releases a quick large amount of energy
transfers within cells