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Biology (Grade 12) > Proteins, Enzymes, & Nucleic Acids > Flashcards

Proteins, Enzymes, & Nucleic Acids Flashcards

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1
Q

What is competitive inhibition?

A
  • inhibitors that compete with the substrate molecules for the active site
  • action is proportional to its concentration; when more inhibitor is present compared to substrate, it will out-compete the substrate for the active site
  • resembles the substrate structure closely
  • no induced fit and no catalyze
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2
Q

How many hydrogen bonds are between DNA?

A

2 hydrogen bonds between A-T
3 hydrogen bonds between G-C

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3
Q

What is a phosphodiester bond

A

~the covalent bond between nucleotides
~ a result of the condensation reaction between the phosphate group of one nucleotide and a hydroxyl group on the sugar of the next nucleotide in the strand
~ one water molecule is produced

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4
Q

What is the tertiary structure of proteins?

A

the helixes and sheets in a polypeptide arrange themselves according to hydrophobic ness/ hydrophilic ness, H-bonding, and electrostatic charges
~ Most of tertiary structure is determined by the hydrophobic effect; polar groups face towards the aqueous environment and non-polar groups towards the interior

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5
Q

What is the active site of the enzyme?

A

region on the protein/enzyme where reactions happen

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6
Q

How is a peptide bond formed?

A

2 amino acids bond, creating 1 water molecule (an oxygen from the carboxyl group and 2 H from the amino group) and a peptide bond which links a carbonyl group to N that is bonded to H

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7
Q

Whats the quaternary structure of proteins?

A

various polypeptides can join together forming multi polypeptide proteins (ex. enzymes)
~ 2 or more large polypeptides interact to create a final shape that gives a protein its function

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8
Q

What are nucleic acids made up of?

A

nucleotide monomers bonded together with a phosphodiester bond which creates a sugar-phosphate backbone

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9
Q

Describe the lock and key mechanism regarding enzymes.

A

The enzyme is the lock and the substrate is the key
~ substrate binds to the enzyme (this is called Enzyme-substrate complex) and after the reaction is done, 2 products are produced

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10
Q

What are enzymes

A

proteins that act as biological catalysts, increasing the rate of certain reactions

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11
Q

What is the catalytic cycle for enzymes?

A

once the reaction is complete, the enzyme can go back to work on a new substrate molecule

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12
Q

What is non-competitive inhibition?

A
  • binds to a different site on the enzyme called the allosteric site, which regulates enzyme activity (they prevent the enzyme from working but do not bind to the active site)
  • decreases enzyme activity
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13
Q

For every 2 amino acids, how many water molecules are produced

A

1 water molecule

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14
Q

What are proteins made up of?

A

amino acid monomers that are bonded together with a peptide bond forming a polypeptide

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15
Q

What are the 4 different Nitrogenous bases?

A

Adenine, Thymine, Guanine, Cytosine
~ (A pairs with T, C pairs with G)

In RNA, all are the same except Thyme (Thymine) is replaced by Uracil

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16
Q

What are the two types of nucleic acids? Describe.

A

DNA (deoxyribonucleic acid)
~ contains the genetic info of an organism which is decoded into particular amino acid sequences of proteins
~ contains a modified 5-carbon sugar which only has 4 oxygen atoms instead of 5 (this gives it its name of deoxy)

RNA (ribonucleic acid)
~ contains the genetic information of some virus particles and assists DNA to make proteins
~ is a large polymer that is composed of nucleotides which contain the sugar ribose (a normal 5-carbon sugar containing 5 oxygen atoms

17
Q

What are the 4 levels of protein structure?

A

Primary Structure

Secondary Structure

Tertiary Structure

  • Quaternary Structure
18
Q

What are some factors that cause protein denaturation?

A
  • changes in pH
  • heat
  • exposure to alcohol
  • high salt concentrations
19
Q

What are some factors that affect enzyme activity? explain each.

A
  • temperature (at high temps, proteins denature; at cold temps, the bonds are not flexible enough to allow the substrate to bind)
  • pH (extreme pH levels cause protein denaturation)
  • concentration of substrate & enzyme
  • inhibitors (chemicals that reduce the rate of enzymatic reactions; reduce the enzyme’s ability to interact with its substrate)
20
Q

How do enzymes provide new reaction pathways?

A

by lowering the activation energy required

21
Q

What types of nitrogenous bases are pyrimidines and purines? Give examples.

A

PYRIMIDINES: single-ringed bases (Thymine & Cytosine)

PURINES: double-ringed bases (Adenine & Guanine)

22
Q

What is the secondary structure of proteins?

A

the amino acids hydrogen bond with neighbors, creating coils (alpha helix) or folds (beta-pleated sheets)
~ FOLDING: B sheets created when H-bonds form between 2 parts of the polypeptide chain layered on each other
~ COILING: alpha helix created by H-bonding between every 4th amino acid within a strand

23
Q

What does the structure of a nucleotide include

A

PSN

Phosphate Group
Sugar
Nitrogenous base

24
Q

Are enzymes recyclable?

A

Yes, they can be reused with every subsequent reaction

25
Q

What is the amino acid structure?

A

Ionized amino group on the left bonded to a C (with H bond at top and R bond at bottom) and ionized carboxyl group on the right

26
Q

What is an enzyme’s specificity determined by? What is the active site determined by?

A

the active site; active site is determined by the folding

27
Q

What are enzyme cofactors?

A

a metal ion or mineral needed by some enzymes to help the reaction
~ ex. iron, zinc

28
Q

What is induced fit for enzymes?

A

induced fit is when enzymes adjust their shapes so that the substrate fits perfectly

the enzymes “hug” the substrate

29
Q

What is protein denaturation? Give examples.

A

the breaking of many bonds within a protein molecule that disrupts its shape & stabilizes the highly ordered structure

short & simple: the breaking of bonds

ex: curling/straightening hair, curing meat, cooking

30
Q

What types of reactions can enzymes catalyze?

A

both ANABOLIC (synthesis/condensation) and CATABOLIC (hydrolysis) reactions

31
Q

What is the primary structure of proteins?

A

the linear sequence/order of amino acids
~ amino acid monomers are joined by peptide linkages, forming polypeptide strands

32
Q

What determines function when talking about proteins?

A

shape determines function

33
Q

What are hydrolase enzymes?

A

enzymes that catalyze hydrolysis reactions

34
Q

What’s the difference between RNA and DNA in terms of structure?

A

DNA has a missing oxygen on carbon 2 (hence it has 4 oxygens) and RNA has all 5 oxygens

35
Q

What are coenzymes?

A

organic molecules that assist the reaction (many vitamins are coenzymes)

Biology (Grade 12) (2 decks)

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