Amino acids joined by peptide bonds to form a polypeptide chain, formed by condensation reactions
Condensation reactions = forming of a chemical bond by the elimination of water
Hydrolysis reaction = breaking of a bond by the addition of water
Structure of protein:
primary structure - sequence of amino acid in a polypeptide chain
secondary structure - determined by the arrangement of hydrogen bonds between carboxylic acid and amino group -> folding of the primary structure to give alpha helix and beta-pleated sheets
tertiary structure - specific 3D shape due to folding of secondary structure -> held in place by disulphide bridges (s), ionic bonds (chargedRgroup), hydrogen bonds (between R groups)
quarternary structure - one or more polypeptide chains bonded together -> bonds form between R bonds, same bonding as tertiary
Disulphide bridges = strong covalent bonds form between R-groups containing sulphur atoms
only tertiary and quarternary
Ionic bonds = form between R groups with charges
only tertiary and quarternary
Hydrophobic interactions = when polypeptidechainsfold, hydrophobic R-group cluster close to each other in the interior of the folded chains
doesn’t interact with water
Hydrophilic interactions = R-groups are on the outside,attracted to water
Interact with water
Peptide bonds = join amino acids to form primary structures
Fibrous:
long strands formed from long parallel polypeptide chains joined together
have a structural use
insoluble in water
maximum is secondary structure
e.g. Keratin, collagen
Globular:
often have spherical or globular structure
often carry out metabolicfunctions
can be soluble in water
can be tertiary or quarternary
catalysereactions , enable transport across membranes
e.g. Hormones
Test for Proteins:
Mix Solution with biuret reagent in a boilingtube
Cover the top of the boilingtube and invert it once