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Title: Human proteins
Description: Basic proteins study notes used for first year bachelor of Biomedical science at Queensland University of Technology. Basic foundation for anyone studying or wanting to study biology or medicine at university.

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182 Lecture 2 Proteins
*Make up over 50% of all dry mass* *ORGANIC*
MONOMERS – (amino acids) are joined together in a linear chain
POLYMERS – (polypeptide)
AMINO ACID STRUCTURE –
R-group – 20 different R groups determine: folding, charge, grouping (polarity of side
changes)
Non-polar Amino Acids–hydrophobic (elements are shared evenly)
Polar Amino Acids– hydrophilic (elements are not shared equally)
ACIDIC SIDE GROUPS – negatively charged
BASIC SIDE GROUPS – positively charged

Determines the structure of the protein via the connection of different R- groups
POLYPEPTIDES – begin with amino acid at the N-terminus end and ends with carboxyl at Cterminus end

Connected via peptide bonds created by condensation reactions
Sulphydryl group- SH group on the R group (SH group on 2x cysteins (each) form disulphide
bridge))
Cyclic structure – cause turn in the protein chain
PRIMARY STRUCTURE – sequence AA
SECONDARY STRUCTURE – Folding of alpha helix and beta pleated sheets
TERTIARY STRUCTURE – overall 3D shape of the protein
QUATERNARY STRUCTURE – several polypeptides come together (If protein is open will continue
to Quaternary stage, if closed will stop at tertiary)

ENZYME – substrate comes and binds to the active site where it’s bonds get broken making
absorption of molecule easier
Title: Human proteins
Description: Basic proteins study notes used for first year bachelor of Biomedical science at Queensland University of Technology. Basic foundation for anyone studying or wanting to study biology or medicine at university.