U3A1: 2A relationship between nucleic acids + proteins Flashcards
functions of proteins, amino acid structure, protein structures.
proteome
complete set of proteins expressed by a genome.
biomacromolecule
large, complex structures crucial to the functioning and development of all living organisms. includes lipids, polysaccharides, nucleic acids and polypeptides.
8 functions of proteins
- enzymes (speed up chemical reactions)
- transport (entry + exit of substances from cells)
- structural (supports cell and tissue shape)
- hormones (communication, inducing change) and receptors (recieving environmental signals)
- defence (recognition + destruction of pathogens)
- motor (muscle movement)
- storage (reserve for molecules in organisms)
structure of an amino acid
- central carbon
- hydrogen atom
- amino group
- carboxyl group
- r-group
role of the r-group in an amino acid
each amino acid has it’s own specific r-group. therefore the r-group uniquely determines the identity of a particular amino acid.
condensation polymerisation
process in which a polymer is formed via a condensation reaction. seperate monomers (amino acids) undergo a condensation reaction, forming a polymer (polypeptide chain) and releasing water as a by-product.
primary protein structure
sequence of amino acids in a polypeptide chain. each amino acid is held via peptide bonds.
secondary protein structure
polypeptide chain folds + coils by forming hydrogen bonds between amino acids of different sections.
- alpha-helices: helix shape caused by repulsion between equally charged side chains.
- beta-pleated sheets: polypeptide lengths line up (can be parallel or antiparallel) forming a sheet.
- random coils: irregular structures (join alpha helices and beta-pleated sheets).
tertiary protein structure
polypeptides are folded into their 3D shape by other proteins, and held in position by hydrogen bonds. it is at this structure that proteins may become functional.
quarternary protein structure
2 or more tertiary proteins structures join together.