What are proteins and examples
Polymers of amino acids
Amino acids
Alpha carbon with with amino group( N terminus) and a carboxyl group( C terminus) and a hydrogen
Polypeptide
Amino acids linked together with peptide bonds
Polypeptide vs protein
Polypeptide is just the chain of amino acids
Protein has specific 3D shape and function
4 levels of protein folding
Primary
Secondary
Tertiary
Quaternary
Primary
Particular sequence of amino acids in the polypeptide
- peptide bonds
Secondary
Hydrogen bonds between atoms of the backbone
Alpha helix, beta sheets, random coils
Alpha helix
Projection of side chains in which every 4th amino acid in the helix is attracted
Beta sheets
Repetitive folding
Projection of side chains from plane
Tertiary structure
Interactions of ionic, hydrogen, hydrophobic, and disulfide bonds
Quaternary
Similar to tertiary except it applies to proteins made with multiple polypeptide chains
Cofactor
Non protein chemical group bound to the protein and required for protein function
Nucleus acids
Polymers of nucleotides
Nucleotide
Contains sugar, 1-3 phosphates and a nitrogen base
DNA
Deoxyribonucleic acid
Deoxyribose sugar
Has only one OH
Double helix
Hereditary info
RNA
Ribonucleic acids
Single strand
Ribose sugar
2 OH groups
Instructions for assembling proteins
Nitrogen bases
Pyrimidines: uracil, thymine and cytosine
Purines: guanine and adenine
Backbone
5’ to 3’ alternating sugar phosphate backbone with phosphodiester bonds
3’ end
Free OH
5’ end
Free P group
A-T vs C-G
A-T has 2 hydrogen bonds
C-G 3 hydrogen bonds
Shapes of DNA vs RNA
DNA is double strand double helix
RNA is single strand, with unique shape due to its pairing of base pairs with itself
Conservative change
New AA has same/ similar properties of the old AA
- similar bonds
- minimal effect on function
Non- conservative change
New AA has different properties than the old AA
- different bonds
- affects function