Proteins Flashcards
Unit 2: Biomolecules
What do proteins contain?
Carbon, Hydrogen, Oxygen, NItrogen and sometimes Sulphur
What are proteins composed of?
They are cmoposed of long chains of monomers called amino acids
What do each amino acids contain?
They contain a central alpha carbon linked to an amine group, carboxyl group, and variable (R) group and a hydrogen atom.
What do amino acids differ by?
Amino acids differ in the composition of their variable side chain (R)
How are dipeptide formed?
Two amino acids joined by condensation
How are polypeptide formed?
They are formed by more amino acids being added to the dipeptide
What catalyzes the condensation reactions?
Ribosomes
What is a peptide bond?
Bond linking amino acids together (C-N bond, -NH2 of one amino acid and -COOH of the other)
Define essential amino acid
Acids that animals cannot synthesize (make) and must be obtained from diet
Define non-essential amino acids
Acids that can be made by animals using pathways that transform one amino acids into another
What can shortage of one or more essential amino acids in diet cause?
They can prevent the production of specific proteins
Ribosome’s function in amino acids?
Ribosomes can join amino acids between any pair of the 20 different amino acids
Functions of R groups?
R groups stabilize the 3D shape of proteins
Define denaturation
When there is a conformational change in a protein, they don’t normally return to their original structure, it’s usually permanent
What can cause denaturation?
Heat, due to vibrations in the molecule
Extreme pH
What do R groups determine?
They determine the vehicle properties of amino acids
Define Conformation
3D shape
What decides which level the proteins conforms to
It’s decided by it’s amino acid structure
What do each proteins conforms into determine
It deterines the fuction of the protein?
What are four levels of protein structure?
Primary Structure
Secondary Structure
Tertiary Structure
Quaternary Structure
Primary Structure
Sequence of amino acids
Formed by peptide bonds
Determines/controls the other levels
Secondary Structure
Folds/turns of amino acid sequence upon themselves
Pattern of H bonds between amine and carboxylic groups creates the secondary structure
H bonds give stability
Fibrous proteins
Tertiary Structure
3D folding pattern due to side chain interactions
Polypeptide folds and coils (complex)
Caused by interactions between R groups
Tertiary shape is very important for function
Globular proteins
Quaternary Structure
Interaction between multiple polypetides
Sometimes prosthetic (part that is not an amino acid) groups involved
Classified as fibrous or globular