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Biological Sciences 121 > Chapter 3: Nucleic Acids, Proteins, and Enzymes > Flashcards

Chapter 3: Nucleic Acids, Proteins, and Enzymes Flashcards

1
Q

Nucleic Acids

A

Polymers that store, transmit, and express genetic information

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2
Q

Nucleic acids are made up of what type of monomers?

A

They are made of nucleotides

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3
Q

What are the two types of nucleic acids?

A
  1. Deoxyribonucleic acid (DNA)

2. Ribonucleic acid (RNA)

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4
Q

What does DNA do?

A

It stores and transmits genetic information

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5
Q

What does RNA do?

A

Carries information of amino acids from genes to where proteins are made

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6
Q

Nucleic acids and proteins encoded by DNA and RNA determine what?

A

They determine the metabolic functions of an organism

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7
Q

Nucleotides

A

Are monomers of nucleic acids

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8
Q

What are the three components of nucleotides?

A
  1. Nitrogen-containing base
  2. A pentose sugar (Ribose in RNA or deoxyribose in DNA)
  3. One to three phosphate groups
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9
Q

Nucleosides

A

Are molecules containing nitrogen base and a pentose sugar that doesn’t have phosphate groups

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10
Q

Pyrimidine

A

a 6 membered single-ringed structure

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11
Q

Purine

A

A fused double-ringed structure

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12
Q

What are nucleotide bonded in?

A

Condensation reaction to form phosphodiester linkages

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13
Q

Condensation reactions

A

A chemical reaction where 2 molecules are joined together by a covalent bond to make a larger, more complex molecule, with the loss of a small molecule

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14
Q

Phosphodiester linkages

A

linkage between the 3’(prime) carbon aton of 1 sugar molecule and the 5’ (prime) carbon atom of another

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15
Q

What are the 4 bases of DNA?

A
  1. Adenine (A)
  2. Cytosine (C)
  3. Guanine (G)
  4. Thymine (T)
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16
Q

What are the 4 bases of RNA?

A
  1. Adenine (A)
  2. Cytosine (C)
  3. Guanine (G)
  4. Uracil (U)
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17
Q

DNA is composed of what?

A

They are composed of 2 polynucleotide strands (double-stranded)

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18
Q

What is RNA structure?

A

It is single-stranded and can fold upon itself, forming a variety of structures

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19
Q

Complementary Base Pairing

A

Nitrogenous bases (A, C, G, and T/U) of the DNA and RNA molecules bond with one another and are held together by hydrogen bonds

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20
Q

Transcription

A

When DNA sequence can be copied into RNA

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21
Q

Translation

A

When RNA specifies the amino acid sequence of a protein from transcription

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22
Q

What are the function of proteins?

A
  1. Enzyme
  2. Defense proteins
  3. Hormonal and regulatory proteins
  4. Receptor proteins
  5. Storage proteins
  6. Structural proteins
  7. Transport proteins
  8. Genetic Regulatory protein
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23
Q

Amino Acids

A

Are the building blocks of proteins and are monomers that make up polymers in protein

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24
Q

What are the 2 functional groups in amino acids?

A
  1. Nitrogen-containing amino acid group (base)

2. the (acidic) carboxyl group

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25
Q

What are the following structural properties of amino acids?

A

They have an alpha carbon, a hydrogen atom, and a R group (side chain)

26
Q

R Group

A

is the fourth bonding electron that is shared with a group that differs in each amino acid

27
Q

What number of amino acids occur in proteins of all living organism?

A

There are 20 amino acids

28
Q

What are the 4 different types of R-Group?

A
  1. Amino acids with electrically charged hydrophilic side chains
  2. Amino acids with uncharged side chains (hydrophilic)
  3. Special cases (Cysteine, Glycine, proline)
  4. Amino acids with nonpolar hydrophobic side chains
29
Q

Amino acids are linked by what?

A

Linked in a condensation reaction to form peptide bonds

30
Q

Peptide Bond

A

Is a chemical bond formed between 2 molecules when the carboxyl group of one molecule react with the amino acid group of the other molecule, releasing a water molecule

31
Q

Where does polymerization take place?

A

It takes place in the amino to carboxyl direction

32
Q

Primary structure of a protein

A

Established by covalent bonds and is the sequence of amino acids in the linear polypeptide chain

33
Q

Secondary structure of a protein

A

It consists of repeated spatial patterns in different regions of polypeptide chain

34
Q

What are the 2 types of second structure of a protein that are determined by hydrogen bonding?

A
  1. alpha helix, which is a right-handed coil that turns the same direction
  2. Beta pleated sheet, which is formed from 2 or more sequences of amino acids that are extended and aligned
35
Q

Tertiary Structure of a Protein

A

Is a three-dimensional shape of a protein that has a singular polypeptide chain (Backbone) made from the combination of alpha-helix and beta-pleated sheet

36
Q

Quaternary structure of a protein

A

have 2 or more polypeptide chains (subunits) bind together by hydrophobic and ionic interactions and hydrogen bonds. (basically means proteins interact with each other)

37
Q

Protein structure can change by what factors?

A
  1. Temperature
  2. Alterations in pH
  3. A high concentration of polar substances
  4. nonpolar substances
  5. molecule interactions that disrupt the interaction between R groups
38
Q

Free Energy Equation

A

Describes the energy change associated with a chemical reaction

39
Q

Catalysts

A

Are substances that speed up reactions without being permanently altered

40
Q

Enzymes

A

Are biological catalysts that are mostly protein, except RNA molecules, called ribozymes

41
Q

What is E_a?

A

is the activation energy required for a reaction to begin?

42
Q

Substrate

A

Are reactants that bind to a specific site on the enzyme

43
Q

Active Site

A

A specific site on the enzyme where the reaction occurs

44
Q

Enzyme-substrate complex (ES)

A

The binding of a substrate to the active site of an enzyme that are held together by H-bonding, electrical attraction, or temporary covalent bond

45
Q

Cofactors in Enzymes

A

Are molecules that some enzymes require to function

46
Q

Coenzymes

A

Have a carbon-containing (organic) molecule that is required for the action of 1 or more enzymes

47
Q

Prosthetic groups

A

non-amino acid groups such as heme, flavin, retinal. Are organic molecules that are permanently bound to their enzymes

48
Q

Substrate concentration affects what?

A

It affects the rate of an enzyme-catalyzed reaction

49
Q

What is the protein tertiary structure sensitive to?

A

It is sensitive to the concentration of H^+ (pH) in the environment

50
Q

What affects enzymes speed?

A
  1. Warming increases rates of chemical reactions, but if the temperature is too high, non-covalent bonds can break and inactivate enzymes
  2. pH levels
51
Q

What can enzymes be regulated by?

A

Inhibitors

52
Q

Chemical inhibitors

A

They bind to enzymes and slow reaction rates

53
Q

Natural inhibitors

A

Regulates metabolism

54
Q

Artificial Inhibitors

A

Are used to treat diseases, kill pests, and help study enzyme function

55
Q

Irreversible Inhibition

A

Inhibitor covalently binds to an amino acid side chain at the active site of an enzyme and it permanently blocks the active site

56
Q

Reversible Inhibition

A

The inhibitor can separate from the enzyme, allowing the enzyme to function fully as before

57
Q

Competitive inhibitor

A

Competes with a natural substrate for the active site, meaning that natural substrate can’t enter the active site

58
Q

Noncompetitive inhibitor

A

Binds at a site distinct from the active site which changes the shape of enzyme and function

59
Q

Allosteric Regulation

A

The non-substrate molecule binds or modifies other than the active site (the allosteric site, causing a change in enzyme shape and active site shape) and alters enzyme activity

60
Q

Allosteric regulation can do what?

A

They can activate/ inactivate enzymes and can be modified by covalent/noncovalent bonding

61
Q

Feedback Inhibition

A

inactivates the enzyme and is a widespread type of enzyme regulation and prevents a cell from making excess products it doesn’t need

Biological Sciences 121 (20 decks)

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