proteins and enzymes Flashcards

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1
Q

what is the monomer of protein?

A

amino acid

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2
Q

what two general structures are part of an amino acid?

A

carbonyl group C=C-O-H and amine group H-N-H

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3
Q

what is formed when two amino acids join together?

A

dipeptide

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4
Q

what is the R group in an amino acid?

A

the variable group responsible for unique properties

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5
Q

how are polypeptides formed?

A

condensation reaction

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6
Q

when does the reverse reaction happen?

A

digestion

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7
Q

what is primary structure?

A

the sequence of amino acids that make up a polypeptide chain

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8
Q

what are the two secondary structures?

A

alpha helix (hydrogen bonds cause it to coil) and beta pleated sheet

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9
Q

what is tertiary structure?

A

the structure is coiled or folded more and more hydrogen and ionic bonds form. disulphide bridges also form between cysteine. if a proteins made from a single polypeptide chain tertiary structure is their final 3D structure

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10
Q

what is quaternary structure?

A

some proteins are made from several polypeptide chains held together by bonds and the quaternary structure is the way they’re assembled together.

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11
Q

how would you test for protein?

A

test solution needs to be alkaline so add a few drops of sodium hydroxide solution then add copper sulfate solution. positive = purple negative = blue

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12
Q

what are some functions of proteins?

A

enzymes, antibodies, transport proteins and structural proteins

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13
Q

what is known as a successful collision?

A

the enzyme and substrate collide and the substrate temporarily binds to the active site

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14
Q

what is formed after a successful collision?

A

the enzyme substrate complex

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15
Q

wha is activation energy?

A

the energy required to start the reaction

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16
Q

what is a competitive inhibitor?

A

a molecule that has a similar shape to the substrate which means it can fit in the active site and stop the reaction

17
Q

what is a non competitive inhibitor?

A

it binds to another area of an enzyme altering the tertiary structure and changing the active sites shape so the substrate can’t fit

18
Q

what is the area the non competitive inhibitor binds to called?

A

the allosteric site

19
Q

what five factors affect enzyme controlled reactions?

A

temperature, pH, substrate concentration, enzyme concentrations conc of inhibitors