Module 2: Biological Molecules - Proteins Flashcards
What are Proteins?
Proteins are polymers of amino acids joined together by peptide bonds.
How many Amino acids does our body need to stay healthy?
20 different amino acids.
What is a Dipeptide?
A dipeptide is formed when two amino acids join together.
What is a Polypeptide?
A polypeptide is formed when more than to amino acids join together.
What elements do Proteins contain?
Carbon.
Oxygen.
Hydrogen.
Nitrogen.
Sulphur.
What is the general structure of amino acids?
They consist of a central carbon atom attached to four different groups:
an amine group,
a hydrogen atom,
a carboxyl group and an ‘R’ group which is different in each amino acid.
Explain the ‘R’ group.
The identity of the R group will influence how the amino acid interacts with other amino acids, therefore influencing protein folding.
Describe the formation of Dipeptides/Polypeptides.
Amino acids join together by peptide bonds to form Dipeptides and Polypeptides. When they join the OH from the carboxyl group on the first amino acid joins with the hydrogen atom on the second amino acid.
This allows a molecule of water to be released therefore it can be called a condensation reaction.
Describe the breakdown of dipeptides/polypeptides.
A molecule of water is added to a dipeptide/polypeptide to break peptide bonds. Two amino acids will be formed therefore it can be called a hydrolysis reaction.
What are the 4 stages of folding a protein undergoes?
Primary.
Secondary.
Tertiary.
Quaternary.
Explain the Primary structure of proteins.
Primary structure of a protein is the order and number of amino acids in a protein.
Peptide bonds have formed between amino acids to form a long, straight chain (polypeptide).
The Primary structure of a polypeptide is determined by the DNA sequence of the gene which encodes that polypeptide.
Explain the Secondary structure of a protein.
Along the polypeptide chain they are -NH and -OH groups which have a slightly negative (OH) and positive (NH) charge.
This causes the groups to attract resulting in hydrogen bonds forming between amino acids.
The hydrogen bonds cause the polypeptide chains to twist and fold into shapes- Alpha Helix or Beta pleated sheets.
Explain the Tertiary structure of a protein.
More bonds form between the different R groups to give the protein a 3D structure. R-group interactions involve hydrogen bonds, disulfide bonds, ionic bonds and polar interactions.
It is the 3D shape of the protein. It can be globular or fibrous
Describe the bonds present in the Tertiary structure of proteins.
-ionic bonds.
-disulfide bridges.
Ionic bonds =
these are attractions between negatively/positively charged R groups on different parts of the molecule.
Disulfide bridges =
when two amino acids of Cysteine join together, disulfides bonds are formed. (strong covalent S-S bonds)
Describe the bonds present in the Tertiary structure of proteins
-hydrophobic/hydrophilic interactions.
-hydrogen bonds
Hydrophilic/Hydrophobic interactions =
When hydrophobic R groups are close together in a protein, the clump together.
This means that the hydrophilic R groups are likely to be pushed on the outside, which affects the protein structure.
Hydrogen bonds =
Weak bonds that form slightly positively charged hydrogen atoms in some R groups and slightly negatively charged atoms in other R groups on the polypeptide chain.