Proteins + nucleotides+ nucleic acids- biological molecules Flashcards
Made up of (elements)
-carbon, hydrogen, oxygen, nitrogen
peptides
polymers made up of amino acid molecules (the monomers)
What do proteins consist of
- one or more polypeptides arranged as complex macromolecules
- they have specific biological functions
essential vs non essential amino acids
- 20 commonly found in cells, five are non essential as our bodies are able to make them from other amino acids,
- 9 are essential and can only be obtained by what we eat
- further 6 said to be conditionally essential as they are needed for growing children
synthesis of peptides
- amino acids join when the amine and carboxylic acid groups connected to central carbon atoms react
- r groups not involved yet
- the hydroxyl in carboxylic acid group of one amino acid reacts with a hydrogen in the amino group of another amino acid
- peptide bond is formed between and h2o is produced (condensation reaction)
- resulting compound is a dipeptide
polypeptide
- when many amino acids are joined together by peptide bonds
- catalysed by the enzyme peptidyl transferase present in ribosomes
primary structure- protein structure
- the sequence in which the amino acids are joined
- the particular amino acids in the sequence will influence how the polypeptide folds
- peptide bonds only
secondary structure- protein structure
- O2, H, N atoms of amino acids interact
- hydrogen bonds may form within the amino acid chain, pulling it into a coil shape called an alpha helix
- or can form beta pleated sheets when polypeptide form hydrogen bonds lying parallel
tertiary structure- protein structure
- folding of a protein into its final shape
- the coiling or folding in their secondary structures brings r groups closer together so they are able to interact and further folding will occur
Interactions between R groups (4)
- hydrophobic and hydrophilic interactions (weak interactions between polar and non polar R groups)
- hydrogen bonds (weakest bonds formed)
- ionic bonds (form between oppositely charged R groups)
- disulphide bonds ( covalent and strongest of the bonds, only form between R groups that contain sulphur atoms)
quaternary structure-protein structure
- results from the association of 2 or more individual proteins called subunits-
- enzymes consist of 2 identical subunits whereas insulin has 2 different subunits
- haemoglobin has 4 subunits made of 2 sets of 2 identical subunits
hydrophilic and hydrophobic interaction affect on the way a protein will fold
- proteins assembled in aqueous environment of cytoplasm
- will depend on if R groups are hydrophilic or hydrophobic
- hydrophilic on outside of protein, hydrophobic on inside
Steps of DNA replication
-The double helix unwinds and the hydrogen bonds between the complementary
bases break using DNA helicase thus separating the two strands of DNA
-Both strands are used as templates and
complementary base pairing occurs between the template strands and free nucleotides
-Adjacent nucleotides are joined by phosphodiester bonds formed in condensation reactions using DNA polymerase
Twenty different amino acids are commonly used for protein synthesis. In theory, this
would need only 20 different base combinations.
Explain the uses of the remaining 44 combinations.
- several code for one amino acid
- some are used to stop terminations
Which nucleotide bases are common to DNA and RNA?
Adenine, cytosine, guanine