A2- Proteins and Enzymes Flashcards

1
Q

What region of amino acids are basic?

A

NH2

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2
Q

What region of amino acids is acidic?

A

COOH

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3
Q

What is a zwitterion?

A

a ion with separate positively and negatively charged groups (overall neutral charge)

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4
Q

When do amino acids form zwitterions?

A

isoelectric point (usually around pH 6)

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5
Q

What happens when amino acids are in alkaline conditions?

A

COOH dissociates, forming COO-

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6
Q

What happens when amino acids are in acidic conditions?

A

NH2 gains H+, forming NH3+

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7
Q

What is the primary structure of a protein?

A

sequence of amino acids

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8
Q

What is the secondary structure of a protein?

A

Hydrogen bonds cause B-pleated sheets or a-helix to form

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9
Q

When does a-helix form?

A

when NH2 groups are on the same side

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10
Q

What is the tertiary structure of a protein?

A

hydrogen, ionic and disulfide bonds make 3D shape

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11
Q

What is an enzyme?

A

protein-based biological catalyst, that speeds up rate of reaction by lowering Ea

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12
Q

Why are enzymes specific?

A
  • a specific active site that must fit and have intermolecular forces with a specific substrate.
  • This promotes the movement of electrons which lowers Ea
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13
Q

What is meant by the term ‘stereospecific’?

A

so specific that only one out of a pair of enantiomers will bind to the enzymes active site

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14
Q

How can enzymes be denatured?

A

changing temp and pH

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15
Q

Explain protein structure…

A

primary:
peptide bonds between amino acids, the specific sequence of amino acids
secondary:
H bonds between amino acids in same chain
alpha helix: Hydrogen bonds between peptide bonds every 4 amino acid residues, on the same chain
Beta pleated sheet: protein folds, hydrogen bonds between parallel peptide bonds
tertiary:
ionic between COO- and NH2 in R groups
disulfide; S-S
hydrogen, BETWEEN R GROUPS
VdWs: Between alkyl side groups

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16
Q

What reagent can be used for protein hydrolysis? Is this reaction fast or slow?

A

conc HCl, slow

17
Q

What locating agent can be used to identify amino acids in TLC?

A

ninhydrin

18
Q

Why might 2 dimensional TLC be used?

A

as some amino acids have similar Rf values in different solvents