MOLECULES AND CELLS Flashcards
Monosaccharide examples
a glucose (OH low) and b glucose (OH high), fructose
Disaccharides definition
Formed when two monosaccharides join by condensation reaction (broke down by hydrolysis)
Disaccharides example
maltose (2 a glucose with a a1,4-glycosidic bond) and sucrose (a gluocse and fructose)
Polysaccharides examples
Starch, glycogen and cellulose
Starch types
Amylose- (a1,4-glycosidic bonds) chains are coiled to form a spiral, held together by H bonds, branched
Amylopectin- ( a1,4-glycosidic bonds and a1,6-glycosidic bonds) much more branched than amylose
Why is starch such a good storage molecule
-Compact
-Insoluable
Large molecule (will not easily pass through the cell membrane)
-branching= many terminal ends= easily hydrolysed when in high demand
Glycogen structure
The same as amylopectin, just more branched and much shorter. stored in the form of small granules
Glycogen function and location
-Found in animal and fungal cells
-Stored in the liver and muscle cells in mammals for fast hydrolysis= faster energy can be supplied
Cellulose structure
Two b glucose molecules, with every other molecule being inverted (b1,4-glycosidic bonds)
Effects of flipping the monomers in cellulose
-Unbranched chains are straighter
-Hydrogen bonds can form cross-linkages between adjacent chains
Cellulose location
Cellulose chains are grouped together in microfibrils (plant cell walls) increases tensile strength
Lipid properties and types
-Hydrophobic
-triglycerides(fats and oils), phospholipids waxes and steriods
Triglycerides structure
One glycerol is joined to 3 fatty acids by 3 condensation reactions, ester bonds are formed
Saturated fatty acid
Contains the maximum number of hydrogen atoms, carbons are linked by C-C bonds (no double bonds)
Unsaturated fatty acids
Have at least one C=C bond in the chain
-Monounsaturated (1 C=C)
-Polyunsaturated (>1 C=C)
Triglyceride functions
-Energy store
-Insulation
-Buoyancy
Phopholipid structure
Instead of 3 fatty acids (hydrophobic), one is a phosphate group (hydrophillic)
Protein structure
-Amino acids are linked by peptide bonds by condensation reactions between the amino and carboxyl group
-Two amino acids joined is a dipeptide
-Many amino acids is a polypeptide
Primary protein structure
Sequence of amino acids in the polypeptide chain
Secondary protein structure
a-helix or b-pleated sheets
Tertiary protein structure
Further folding of the secondary structure, this gives it it’s 3D shape
-Hydrogen bonds
-Ionic bonds
-Disulfide bonds
-Hydrophobic interactions
Quaternary structure
Two or more polypeptide chains bonded together
Fibrous proteins
-Collagen
-Found intendons that link muscle to bone
Globular proteins
Have a metabolic role and include enzymes and antibodies. Haemoglobin is an example