Biomolecules Flashcards
What is the monomer of proteins
Amino acids
What is the structure of amino acids?
A central carbon atom(a-carbon) covalently bonded to 4 groups
- basic amine group (-NH2)
- acidic carboxyl group (-COOH)
- a hydrogen atom
- a variable group, R group
What are the properties of amino acids?
- Non-polar (Hydrophobic)
e.g glycine, valine, methionine - Polar (hydrophilic)
e.g cysteine - Charged (hydrophilic)
e.g glutamic acid
*charged ≠ polar
How are the properties of amino acids affected by?
The R-group vary in size and charge and this gives the amino acid its unique chemical properties.
chem properties influence types of bonds btw amino acids -> how a protein folds-> affects its 3D configuration -> function
In an aqueous solution, amino acids exist as …
zwitterions
- carries both negative and positive charges on different atoms but has total net charge of zero (electrically neutral) -> dipolar ion
- amphoteric
In neutral aq solution, amino acids act as …
buffers , resisting small changes in pH when an acid or alkali is added by taking up or losing protons (H+)
When amino acids bond to each other and form proteins, do they still act as buffers?
Buffering properties are still retained because of the basic and acidic R groups of individual amino acids.
How is a polypeptide formed?
Amino acids are joined together via peptide bond to form polypeptide
Describe the formation of the peptide bond
It is a covalent bond formed btw the amino group of one amino acid and the carboxyl group of another via a condensation reaction, with the loss of a water molecule, catalysed by peptidyl transferase
Describe ionic bond
Bond (electrostatic attraction) formed btw basic and acidic R groups of amino acids
Describe disulfide bond
It is a covalent bond (STRONG) formed between sulfhydryl groups (-SH)
- only amino acid cysteine contains -SH in its R group
Describe hydrogen bond
It is a relatively weak, non-covalent bond between an electronegative atom (F,O,N) and a hydrogen atom attached to another electronegative atom.
Describe hydrophobic interactions
Occur btw non-polar or hydrophobic R groups
-formed at the core of the proteins
What are the types of bonds that hold a protein in shape?
- hydrogen bonds
- ionic bonds
- disulfide bonds
- hydrophobic interactions
What is the feature of reducing sugars?
They contain free ketone/aldehyde groups