Their difference in sugars (deoxyribose and ribose)
DNA is double-stranded, whereas RNA is single-stranded
DNA has base Thymine, whereas RNA has base Uracil
Give a brief description of tRNA?
Carries an specific amino acid
Contains an anticodon, a complementary code that binds with codons from mRNA to release amino acids from tRNA and form a peptide through condensation polymerisation
Synthesised in the nucleus
Give a description of rRNA?
Combines with proteins to form the main structural component in ribosomes
Make up the large & small subunits in ribosomes
Synthesised in the nucleolus
What is the structure of DNA?
Double helix
Phosphate sugar backbone formed by a phosphodiester bond (strong covalent bond)
Antiparallel
Complementary base pairing
Adenine contains two hydrogen bonds with Thymine/Uracil
Guanine contains three hydrogen bonds with Cytosine
Which of the following are purines (two carbon nitrogen ring bases)/pyrimidines (one carbon nitrogen ring base)?
Purines: Adenine & Guanine
Pyrimidines: Cytosine & Thymine & Uracil
Explain condensation polymerisation of nucleotides
The reaction that joins nucleotides together is know as a condensation polymerisation reaction
The bond that combines phosphate & sugars is a phosphodiester bond
When phosphate and sugar bonds, a molecule of water is released (condensation) making a polymer (polymerisation), forming the phosphodiester bonds
What is a proteome?
The complete set of proteins expressed by the genome of an individual cell or organism
Primary Structure
Sequence of amino acids
The shape of the protein, and therefore its function is determined by the primary structure (because of the sequence of amino acids)
Held together by peptide bonds
Secondary Structure
When a polypeptide chain folds and coils by forming hydrogen bonds between peptide backbones of amino acids
Secondary structure is characterised by alpha helices, random coiling and beta pleated sheets
Random coils - Irregular section of the polypeptide that form between alpha helices and beta pleated sheets
Tertiary Structure
Proteins fold into their 3D shape due to the characteristics of the amino acids in the polypeptide chain
There are several types of bonds responsible for this:
Hydrogen bonds form between R groups
Disulfide bonds form between cysteine amino acids - provides strength and stabilises the 3d structure
Ionic bonds form between charged amino acids
For a protein to be functional, it needs to at least be a tertiary structured protein
The specific shape of a protein determines its function (e.g enzyme, receptor etc)
Quaternary Structure
When two or more proteins of tertiary structure join together
Not all proteins have quaternary structure
Polypeptide chains with a prosthetic group attached are also considered to have quaternary structure
A prosthetic group is a non-protein group such as an ion or vitamin bound to a protein
H H O
I I II
N - C - C - OH
I I <---------- Centralcarbon
H R
Amino R- Carboxyl
Groups
The characteristics of each amino acid are determined by the R-group (E.g an amino acid with a hydrophobic R-group is more likely to form bonds with another amino acid with a hydrophobic R-group)
Amino acids are joined together by peptide bonds formed by condensation polymerisation
During this process, an H2O molecule is released, while a polymer (polypeptide) is formed
Genetic code is:
Universal: Nearly all living organism use the same rules & codons to code for proteins
Degenerate: Different codons can code for the same amino acid
Unambiguous: Codons can only code for a single amino acid
Non-overlapping: Each triplet or codon is read independently of adjacent triplets or codons / each nucleotide is part of only one codon