bio 20 ap Biochemistry/organic compounds

forms through hydrogen bonding when a slightly positive hydrogen attracts to a slightly negative atom like oxygen nearby

hydrogen bonds allow for structural support and its a weak force compared to covalent and ionic bonds

high heat of vaporization- cooling system for animals, universal solvent-breaks down large toxic molecules like ammonia, hydrogen bonds provide liveable life conditions, water can also stick to itself (cohesion) and other substances (adhesion). This gives water its surface tension and the reason it's liquid. As water freezes hydrogen bonds stabilize and it becomes less dense

organic molecules are molecules that contain hydrogen and carbon. Biomolecules are organic molecules used for life functions and they are related because of the carbon properties they all have.

• Single carbon bonds-stable and the bond will determine shape and function
• double carbon bonds- less flexible and the double bond gives it a different shape and function

• a carbon chain that has other atoms attached to it giving it unique properties. a functional group has the same properties regardless of the carbon chain
• hydroxyl, carbonyl,carboxyl, amino, sulphydryll, phosphate

organic molecule that has the same formula but different stucture or arrangement. This means they are usually in different functional groups so different properties.

• macromolecules are many sub units joined together or polymers
• monomers are the sub units

dehydration synthesis is a reaction that builds polymers. hydroxyl of one monomer and hydrogen of a monomer create water while the monomers bond. Water is by product

• hydrolysis- a reaction used to break apart polymers
• water inserts itself between the bonds of the polymer and the oh binds to one sub unit while the h bonds to another sub unit

True

• a source of energy for all living organisms and structural functions for plants too
• storage--- glycogen in animals and starch in plants
• structure--- cellulose in plants and veggies, chitin in some animals and fungi and peptidoglycan in bacteria

• monosaccharides- one sub unit of a larger sugar molecule or a single sugar molecule.
• (carbs can have 3-7 carbons glucose most common hexose)
• disaccharide- a dimer of a monosaccharide 2 monos bonded through dehydration synthesis 
• polysaccharide-polymer of monosaccharides

insoluble in water because of hydrocarbon bonds that are non-polar, many functions like components of cell membrane, hormones and energy storage

• triglycerides are mainly used in energy storage. animals-fats, plants-oil. Composed of a glycerol back bone, and 3 fatty acids 
• the glycerol backbone is composed of 3 carbons and 3 hydroxyl groups, its polar, and becomes non-polar when 3 fatty acids are bonded to it through dehydration synthesis. 
• fatty acids are a long chain of hydrocarbons with a carboxyl group at the end. its slightly acidic and the carboxyl undergoes dehydration synthesis with hydroxyl

• saturated- no double carbon bonds and lots of hydrogens so its stronger and a solid. its hard to break down
• unsaturated- has one or more double bonds so less hydrogens. its weaker and liquid. plus easier to break down. Can become trans fats

• waxes-contain a fatty acid, alcohol functional group, and a carbon chain, Hydrophobic
• phosphates-have two fatty acids and a phosphate group instead of a third fatty acid the tail is fat and non-polar (hydrophobic). While the head is a phosphate and polar (hydrophillic
• steroids/sterols- Are composed of 4 carbon chains joined together with a functional group attached. cholesterol is used to build most hormones.

• monomers- amino acids, over 20 different ones because they have different r groups. proteins range from 8-1000 amino acids 
• polymers- polypeptides, a peptide is bond between amino acids

• dehydration synthesis to join amino acids through covalent bonds
• hydrolisis to break polypeptides into individual amino acids

• primary structure- simple linear chain of amino acids
• secondary- when proteins are folded or coiled depends on location of hydrogen bonds. Fold- beta-pleated sheet, coil- alpha Felix
• tertiary structure-occurs when there is a irregular bond in R-group/backbone. Results in ball like proteins.
• Quaternary structure- happens when two polypeptides are joined together making a larger macromolecule

False

its a nucleotide while carbs have monosaccharides

• denature is when the protein shape is changed but its reversible
• coagulation is when the protein structure is irreversible

• simple uses Benedict reagent. the mono and disacharddies reduce the iron in the reagent as temp increases causing colour change (blue to orangey red)
• advanced uses iodine. amylose of polypeptides bonds to the iodine changing colour (brown to black)

• proteins- beuret solution it reacts with peptide bonds changing colour (blue to pink to purple) more bonds means more reactions means more colour change 
• lipids translucent test and sudan 4 which dissolves in fat changing colour pink to red.

a phosphate, a nitrogen and carbahydrates

• hydroxyl- found in carbs and alcohols 
• carbonyls- found in sugars
• carboxyl- found in fatty acids and amino acids
• phosphates- lipids and dna
• amino- amino acids and nucleic acids
• sulfhydrll- found in amino acids