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Year 12 Biology > Topic 2 > Flashcards

Topic 2 Flashcards

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1
Q

Organic molecules

A
  • contain carbon, hydrogen and oxygen

- most are macromolecules- due to large size

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2
Q

4 types of macromolecules

A
  • proteins
  • lipids
  • carbohydrates
  • nucleic acids
  • all apart from lipids are classified as polymers- link up of smaller repeating monomers, to form long chains- polymers
  • lipids are made of distinct chemical groups of atoms
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3
Q

name of reaction for creating polymers from monomers

A

Condensation polymerisation reaction

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4
Q

polymer

A

very large molecule, composed of a chain of many similar/identical monomers bonded together

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5
Q

Condensation (dehydration) reactions

A
  • putting together
  • endergonic/anabolic reaction- requires energy
  • water is released in reaction
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6
Q

hydrolysis reactions

A
  • breaking apart
  • exergonic/catabolic reaction- energy is released
  • polymer is broken down into its constituent monomers.
  • water is required
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7
Q

Inorganic molecules

A
  • small molecules do not contain all of carbon, hydrogen and oxygen
  • still essential substances for living organisms e.g CO2, oxygen
  • mineral ions are important as they determines osmotic pressure of cell.
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8
Q

Nucleotides

A

monomer of nucleic acid

  • consist of:
  • five carbon sugar (ribose RNA, deoxyribose DNA)
  • negatively charged phosphate group
  • organic nitrogen-containing base
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9
Q

Purine bases

A

Adenine and guanine

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10
Q

Pyrimidine bases

A

Thymine, Cytosine and uracil (RNA only)

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11
Q

Types of RNA

A

transfer RNA (tRNA- transports specific amino acids to ribosomes for incorporation of growing polypeptide chain

  • messenger RNA (RNA)- contains coded information, in groups of 3 bases called codons
  • specify the order of amino acids to be joined together to make protein (mRNA is complimentary to DNA template strand of gene)
  • Ribosomal RNA- many chains of rRNA, together with proteins make up ribosome
  • holds mRNA, tRNA, amino acids and growing polypeptide chain in correct orientation for protein synthesis
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12
Q

differences between DNA and RNA

A

DNA - double stranded, contains deoxyribose sugar, has bases A, G, C, T
RNA- single stranded, contains ribose sugar, has bases A, G, C, U

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13
Q

DNA structure

A
  • two strands of nucleotides, running antiparallel to each other
  • one strand runs 3’ to 5’, other 5’ to 3’
  • sugar of one nucleotide joins to phosphate of next nucleotide
  • occurs through CPR
  • bond between phosphate and sugar- phosphodiester linkage
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14
Q

Chromosome structure

A
  • DNA wraps around proteins (histones) to form chromosome

- as DNA wraps around histones- forms nucleosomes

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15
Q

properties of genetic code

A

triplets on DNA, codons on RNA, anticodons on tRNA

  • degenerate/redundant- each triplet codes for one amino acid- but single amino acids may have more than one triplet coding for it
  • non-overlapping- code doesn’t overlap- 12 bases code for 4 amino acids
  • universal- DNA is essentially same in all known organisms and codons code for same amino acids.
  • start and stop- one start codon and 3 stop sequences
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16
Q

structure of amino acid

A 
amino group NH2
carboxyl group COOH
hydrogen atom
central carbon atom
varying r group
-r group difference distinguishes amino acids/ and change amino acid properties
17
Q

primary structure of proteins

A
  • specific linear sequence of amino acids
  • bonds between amino acids are peptide bonds
  • OH on carboxyl group and H on amino group bond- release water
18
Q

Secondary structure

A
  • once polypeptide chain is formed, various parts undergo folding due to H bonds between amino acids
  • three configs
  • tight coils- alpha helix- tough and flexible
  • folding forms- beta pleated sheets- soft and flexible
  • unchanged- random coils- binding/ active sites of proteins
  • H bonds between amino acids provides strength/stability/ ability to contract/stretch or active site shape contribution
19
Q

Tertiary Structure

A
  • total irregular folding- held together by ionic or hydrogen bonds- forms complex shape
  • based on r groups-amino acids have different properties
  • hydrophilic attracts hydrophilic
  • negative attracts positive
  • causes polypeptide chain to become folded, coiled or twisted- forms 3D shape-determines function of most protein.
  • tertiary structure determined by hydrogen, ionic or disulphide bonds and r group interaction or adjacent amino acids
20
Q

quaternary structure

A

-consists of two or more polypeptide chains

21
Q

types of conjugate proteins

A

nucleoproteins- (protein + nucleic acid) found in nucleus
lipoproteins- (protein+ lipid) found in membrane
glycoproteins- (protein + carbohydrate)- plays important roles in cell recognition and cell defense mechanisms
chromoproteins- (proteins + pigments)
metalloproteins- (proteins + metal elements)

22
Q

Denaturation

A
  • process in which a protein unravels and loses its native conformation, thus becoming biologically inactive
  • caused by high temperature, strong acid/base, strong salt.
  • these cause protein to denature- irreversible
23
Q

proteome

A

complete array of proteins produced by single cell of organism in particular environment

24
Q

genome

A

complete set of genes carried by organism

Year 12 Biology (16 decks)

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