Biological Molecules: Proteins Flashcards
Secondary protein structure - the Alpha Helices
Polypeptide winds into helix, creating a very stable structure
Secondary protein structure
This is the way the primary polypeptide chain folds and coils: this forms a beta pleated sheet or alpha helices. The bonds forming these structure are hydrogen bonds.
Protein functions
Toxins (e.g diphtheria toxin)
- Antifreeze (e.g glycoproteins in arctic fleas)
- DNA
- Lubrication (e.g glycoproteins)
- Hormones (e.g insulin)
- Enzymes (e.g amylase)
- Pumps (e.g Na + pump in cell membrane)
- Storage (e.g albumins in egg)
- Receptor (e.g motor neurons/rhodopsin)
- Blood clotting (e.g fibrin)
- Stucture (e.g collagen in bone)
- Antibodies (e.g immunoglobulins)
- Motors (e.g myosin in muscles)
Protein composition
Always contains elements carbon, hydrogen, oxygen and nitrogen.Proteins are the most diverse and important group of biological compounds
Primary structure
The sequence of amino acids in the polypeptide chain:
- This is the sequence of amino acids that makes a polypeptide chain, held by peptide bonds
- Primary structure determines the ultimate shape of the protein
- Peptide bonds maintain the structure
- Limitless number of combinations so protein varies considerably
Tertiary protein structure
The way the polypeptide folds into a unique and specific 3D shape. There are limitless possibilities.
Quaternary structure
Proteins made of more than one polypeptide structure joined together e.g haemoglobin and antibodies
Secondary protein structure - the beta pleated sheet
Polypeptide chain zig-zags forming a pleated sheet. Formed by hydrogen bonds.