Proteins Flashcards
Most abundant biomolecule in cytoplasm
Proteins
Primary structure:
1st amino acid
Last amino acid
What can we identify
N terminal - to the left
C terminal - to the right
Only protein structure where sequence of amino acids can be identified
Secondary structure:
Alpha helix - examples/ bond
Collagen, alpha keratin / intramolecular hydrogen bonds between 1st and 4th amino acid
Secondary structure
Beta pleated sheet - example/bond
Beta keratin - parallel/ in reptiles and birds
Fibroin - antiparallel/ in web of spider and silk fibre
Intermolecular H bonds
Tertiary structure examples
Most enzymes, myoglobin, cytochrome
Quarternary structure examples
Haemoglobin, DNA polymerase, ion channels (trans membrane proteins)
Fibrous proteins
Secondary structure proteins develop structural components or fibres or cytofilaments, and hence, are called fibrous proteins
Globular/Functional Proteins
Tertiary and quarternary proteins exhibit specified functions like ion transport, catalysis, storage
Simple proteins
Polymer of amino acids only Albumin Pepsin Trypsin Histone
Conjugated protein
Complex of protein and non protein subunits
Haemoglobin ( 4 haem and 4 protein chains)
Myoglobin ( 1 haem and 1 protein chain)
Casein ( phosphate and protein chain)
Chylomicron ( phospholipid and protein chain)
Transporter proteins
Assists in material exchange and transportation GLUT 4 (insulin-dependent glucose transporter) SGLT ( Sodium glucose co transporter) haemoglobin and trans membrane channel proteins
storage proteins
Stores nutrients or other essential substances
Myoblobin stores O2
Ferritin stores Fe2+ in liver
Therapeutic proteins
Help in healing or homeostasis
Renin and albumin (osmoregulation)
Prothrombin and fibrinogen (clotting protein)
Antibodies (antigen inactivation)
Catalytic proteins
Catalyse biochemical reactions
Enzymes
Acidic proteins
Acidic amino acids are abundant and impart negative charge
Most plasma proteins
Cytoplasmic proteins