3.1 Biological Molecules Flashcards
What is an isomer?
Same chemical formulae, different arrangement
Monomers making Maltese?
2 glucose
Monomers making Sucrose?
Glucose + Fructose
Monomers making Lactose?
Glucose + Galactose
Bonds between sugars
Glycosidic
Isomers of glucose
Alpha glucose
Beta glucose- flip on carbon 1, alternating directions when in chain
Starch
Alpha glucose (stored on plants)
- mostly unbrancged and tight helix shape
- insoluble, compact, easily hydrolized, large molecule
Glycogen
Alpha glucose (stored in animals)
- short and branched, tight helix shape
- insoluble, compact, lots of ends for hydrolysis, large molecule
Cellulose
Beta glucose (cel walls)
- straight and unvranched, parrelel chains connected by hydrogen bonds
- Cross links so collectively strong, microfibrels and fiberals for more stregnth
- stops cell from wilting
Test for reducing sugar
2cm³ of food sample +Benedicts solution+ heat
Colour change blue to red (shows concentration by colour)
Testing for non reducing sugars
2cm³ of food sample + 2cm³ of HCl (hydrolize into monomers)
+ NaHCO3 (neutralize)
Then perform reducing sugars test
Test for Starch
Drops of iodine on 2cm³ of food sample
Colour change brown to blue/black
Colorimeter in test for sugars
tests solutions absorbance of light
- more intence the colour more absorbant it is
- need to caliberate device with water and known concentrations glucose (Quantative Data)
7 Functions of protiens with examples
- contractile (actin+myosin, cilia+flagellum)
- storage (ovalbumin (egg white) and in seeds)
- receptor and hormonal (nerve membrane and insulin)
- transport (haemoglobin)
- enzymatic (digestive enzymes)
- structural (silk fibers for webs, collagen and elastin, keratin for hair/feathers/horns)
Amino acid structure and properties of R groups
NH2-CHR-COOH (amine and carboxly group)
-20 natural occurring amino acids
R groups can be:
hydrophilic (charged) or hydrophobic
-acidic, basic or amphoteric (acid and base so used as buffers)
Simple protien
Made if only amino acids
Conjuncted protiens
Contain amino acids and a non-Amino acid part called “prosthetic group”
Primary structure of protiens
The sequence of amino acids joined by peptide bonds
-change to primary structure due to mutations in DNA
Secondary structure of protien
The way the polypeptide chain is folded into ALPHA HELIX or BETA PLEATED SHEETS
-joined by weak Hydrogen bonds
-chain can have some regions coiled and others folded
Tertiary structure of protiens
Protien folds further to give molecule a globular shape
- forms specific 3D shapes
- important for enzymes and antibodies
Types of bonds in tertiary structure of protien
Ionic- NH2 • • •COOH, broken by pH change
Hydrogen- strong in number, broke by temp or pH change
Disulphide- strongest bond in structure (S‐S)
Hydrophobic interactions- hydrophobic R group cluster together in presence of water (not a bond)
Structure of DNA
- nucleotide (phosphate group, deoxyribose pentosugar, nitrogeonous base)
- joined by PHOSPHODIESTER BONDS
- double helix
Bases and Base interactions
Adenine Guanine (purine) Thymine Cytosine (pyrimidines) A--T C---G Hydrogen Bonds