Proteins, Polysaccharides And Lipids Flashcards
A-helix examples
Haemoglobin, Myosin
A helix bonding
CO hydrogen bonded to NH 4 residues ahead.
3.6 residues / helix turn
A helix structure
Rod. Strong extensible proteins. Stabilised by H bonds
Beta Pleated Sheet example
Proteins where flexibility eg silk fibroin (anti-parallel)
Beta pleated sheet structure
Zigzag chains. Parallel, Anti-parallel
Beta pleated sheets bonding
Chains align, CO and NH align, H bonding occurs = sheet structure
Triple Helix example
Collagen only. Connective tissue (skin, bone, tendon)
Triple helix structure
Strong soluble fibres. Three chains = tropocollagen
Triple helix amino acid number
1000 per chain. No H bonds in chain
Triple Helix chemical structure
X-Pro-Gly or X-Hyp-Gly. H bonds between Hyp and Hydroxylysine residues
Triple Helix 2
Small Gly residues. Bulky R groups point outwards. Intra/inter covalent bonds between Lys and His
Fibrous proteins
Insoluble, metabolically unreactive.
Collagen
Keratin
Fibrin (blood clots)
Elastin (eg arterial walls)
Myosin (muscle)
Physical structure of collagen triple helix
Glycine, hydroxyproline, proline
Globular proteins
Spherical. Backbone folds on itself. Soluble
Globular proteins structure
Usually have 3• and 4• structures eg myoglobin and actin (3•) and haemoglobin (4•)
Sterols examples
Cortisol, Cholesterol, Estrogen (estradiol) , testosterone
Stearic acid (saturated fat and fatty acid)
the molecules are tightly packed
Unsaturated fat and fatty acids (oleic acid)
The molecules cannot pack together closely due to kinks