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Biological Molecules - Coggle Diagram
Biological Molecules
Lipids
-found in olives, peanuts, palm fruits and butter
-AKA fats and oils
-monomer = fatty acids and glycerol( fatty acid tails; and glycerol backbone, which some do not have like steroids)
-non polar
-hydrophobic
-carbon, hydrogen and oxygen; 1:2: very little oxygen
-
-has a polar head and a non polar tail
-found on cell membrane; for selective permeability that regulates the movement of substances in and out of the cell
-
- saturated; unkinked
- unsaturated; kinked
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Nucleic acids
-monomers = nucleotides ( sugar, phosphate, nitrogenous base)
-polymers = nucleic acids
-
DNA
Structure:
-Linear and double stranded in eukaryotes
-circular and double stranded in prokaryotes
consists of;
adenine
thymin
cytosine
guanine
and deoxyribose sugar
location:
found in the nucleus of eukaryotes
found in floating in the cytoplasm in prokaryotes
RNA
single stranded
types:
mRNA
tRNA
rRNA
consists of;
adenine
uracil
cytosine
guanine
and ribose sugar
location:
made in the nucleus transported to the cytoplasm
-
carbohydrates
-
-found in cassava, yam and rice; generally starchy foods
-monomer = monosaccharides( glucose); linked by GLYCOSIDIC BOND/ LINKAGE
-polymers = polysaccharides
-polar
-hydrophilic
-has hexamer ring structure
-carbon, hydrogen and oxygen; in ratio 1:2:1
functions:
-it is a short term energy complex
-it provides structural support; chitin in crabs and mollusks;
cellulose in plant cell wall
- Energy storing carbohydrates
-have a branched structure
can easily be broken; release energy at a faster rate.
- Structural carbohydrates
-have a linear structure and are bale to stack; allowing for a tough structure that allow for structural support
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Proteins
-found in meats, milk and egg
-monomer = amino acids
-polymer = polypeptide
-carbon, hydrogen, oxygen, nitrogen and sulfur.
functions:
-repair of wounded tissues
-catalyzing chemical reactions( enzymes)
-cell signaling( receptor proteins)
-hormones-insulin
-channels- aquaporins, sodium-potassium pump
-transport of materials- hemoglobin for oxygen in blood; myoglobin for oxygen in muscles
-antibodies
-structural support; keratin for hair;
collagen for body tissues
It takes a protein three to four stages;
- Primary
peptide bond( amine-carboxyl linkage) formation between various amino acids.
- Secondary
-folding starts
-we get alpha helices or beta pleated sheets through hydrogen bonding.
- Tertiary
-folding finishes after hydrophobic collapse, ionic bond formation, disulphide bond formation( mostly between cysteine residues) and hydrogen bonding.
- If necessary quaternary
-multiple proteins co me together
-joined by hydrogen bonds
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