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Biology Unit 3/4 > 2. Nucleic Acids and Proteins > Flashcards

2. Nucleic Acids and Proteins Flashcards

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1
Q

What are organic molecules?

A

Molecules that contain all of carbon oxygen and hydrogen

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2
Q

What are the major groups of macromolecules

A

Nucleic acids
Proteins
Carbohydrates
Lipids

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3
Q

What is a polymer

A

A polymer is a very large molecule composed of a chain of many similar or identical monomers which have bonded together

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4
Q

How is a polymer made

A

Proteins, nucleic acids and complex carbohydrates are built up by linking smaller repeating molecules called monomers to form long chains called polymers. Reactions of this kind are termed polymerisation reactions.

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5
Q

Why are lipid not polymers

A

Lipids are not polymers as they are composed of distinct chemical groups of atoms

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6
Q

What is a condensation reaction

A

Dehydration reaction
A polymer is formed when monomers are linked together in condensation reactions. Energy is required, endergonic reaction and water is released.

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7
Q

What are hydrolysis reactions?

A

In a hydrolysis reaction a polymer is broken down into its monomer constituents. Energy is released and water is required.

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8
Q

What are inorganic molecules

A

Small molecules that do not contain all of carbon oxygen and hydrogen.
Example, oxygen carbon dioxide water and salts and mineral ions.

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9
Q

What do nucleic acids do

A

Store information in a chemical code that directs the machinery of the cell to produce proteins. Two types DNA and RNA

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10
Q

What are nucleotide made up of

A

They are the monomers that make up DNA molecules. Composed of a five carbon sugar (ribose in DNA and deoxyribose in DNA)
A negatively charged phosphate group
And organic nitrogen containing compound called a base

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11
Q

What does rna consist of

A

A chain of rna nucleotides joined by phosphodiester bonds

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12
Q

What is transfer rna

A

A single folded chain of rna that transports specific amino acids to the ribosomes for incorporation into the growing polypeptide chain.

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13
Q

What is messenger RNA

A

A single chain of RNA that contains the coded information in groups of three bases called codons that specify the order of amino acids to be joined together to make a protein. mRNA is complementary to the DNA template chain of a gene.

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14
Q

What is ribosomal RNA

A

Many chains of rRNA and proteins make up a ribosome, the site of protein synthesis. The ribosome holds the mRNA tRNA amino acids and growing polypeptide chain in the correct orientation for protein synthesis

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15
Q

Structural differences between DNA and RNA

A

DNA has double chains RNA has single
DNA has deoxyribose sugar RNA has ribose sugar
DNA has bases actg RNA has bases gcua

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16
Q

What is the structure of DNA

A

Consists of two nucleotide chains in opposite direction. One chain of nucleotides turns head to tail with the phosphate group at the head, the 5 prime end. The sugar group at the tail end, 3 prime. The numbers correspond to the carbon number in the sugar molecule. Two chains are antiparallel

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17
Q

What is the backbone of DNA

A

In each chain the sugar of one nucleotide is joined to the phosphate of the next nucleotide to form the backbone.
This occurs through condensation polymerisation reaction
DNA backbone is alternating sugar and phosphate grounds
The 5’ phosphate group of one nucleotide forms a phosphodiester linkage with the 3’ hydroxyl of the sugar groups of the adjacent nucleotide in the chain.

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18
Q

What is the structure of chromosomes

A

The DNA double helix combines with certain proteins called histones. The the DNA winds around clusters of histone proteins it forms structures called nucleosomes.

19
Q

What is the triplet code

A

The code is read in a sequence of three bases called triplets in DNA, codons in mRNA and anti codons on tRNA

20
Q

Why is the genetic code redundant

A

More than one triplet code codes for one amino acid

21
Q

Why is the genetic code universal

A

DNA is said to be a universal indicator of life because the code is essentially the same in all known organisms and the codons code for the same amino acids

22
Q

What do proteins do

A

Contribute to the building of many different structures and parts of a cell and as catalysts control life processes

23
Q

What do proteins contain

A

Carbon oxygen hydrogen and nitrogen, may contain sulphur

24
Q

What is the monomer for proteins

A

Amino acids

25
Q

How many amino acids are there

A

There are 20 naturally occurring amino acids. Plants can synthesis their own amino acids but animals depend on obtaining them from their food. In humans 9 amino acids are essential in the diet, the other can be made from pre existing amino acids

26
Q

What is the structure of amino acids

A

Central carbon atom to which are attached a hydrogen atom, carboxyl group, amino group and an r group

27
Q

What makes amino acids unique

A

The r group distinguishes one amino acids from another, changing their properties

28
Q

What is the primary structure of proteins

A

The specific linear sequence of amino acids in the polypeptide determined by the sequence of bases in DNA.

29
Q

How do amino acids bond

A

In the process of condensation polymerisation. The bond between the two adjacent amino acids is called a peptide bond. The OH on the carboxyl group of one amino acid bonds with the H on the amino group of the adjacent amino acid and water is released

30
Q

What is the secondary structure of proteins

A

The polypeptide chain undergoes folding due to hydrogen bonds that form between various amino acids that are present

31
Q

What are the three configurations of the secondary structure of of protein

A
  • tight coils are known as alpha Helixes which provide tough and flexible properties.
  • folding forms the beta pleated sheets which provide soft and flexible properties
  • unchanged parts of the polypeptide chain are called random coils and usually form binding and active site of proteins
32
Q

What do hydrogen bonds between amino acids do

A

In alpha helix and beta pleated sheets they provide strength and stabile, allowing for contraction or stretching and may contribute to the shape of the active site enabling the protein to carry out its function

33
Q

What is the tertiary structure of proteins

A

Refers to the total irregular folding held together by ionic or hydrogen bonds, forming a complex shape
Hydrophilic r groups attract other hydrophilic r groups
Hydrophobic r groups attract each other
Positive charges are attracted to opposite charges
Fold polypeptide chain into proteins 3D shape determining it’s function

34
Q

What is the quaternary structure

A

Many large complex proteins consist of two or more polypeptide chains

35
Q

What are conjugate proteins

A

Proteins where amino acids bond to non protein compounds

36
Q

Where are proteins modified

A

Proteins are modified in the rough endoplasmic reticulum or Golgi body once they have been produced at the ribosome

37
Q

How does the processing of pre pro insulin to active insulin occur

A
  • prepro insulin is synthesised as a random coil on membrane associated ribosomes
  • after a membrane transport the leader sequence is cleaved off by a protease enzyme and the resulting pro insulin folds into a stable conformation
  • disulphide bonds form between cystein side chains
  • the connecting sequence is cleaved off to form the mature and active insulin molecules
38
Q

What is denaturation

A

A process in which a protein unravels and loses its native conformation the by becoming biologically inactive

39
Q

What causes denaturation

A

Extreme heat, pH extremes, strong salt solutions

40
Q

Proteome

A

The complete array of proteins produced by a single cell or an organism in a particular environment

41
Q

Proteomics

A

The study of the proteome, the complete array of proteins produced by an organism

42
Q

Genome

A

The sum total of all genes in an organism encoded in DNA

43
Q

Genomics

A

The area of genetics concerned with the sequencing and analysis of an organism’s genome

Biology Unit 3/4 (4 decks)

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