Quiz 2 Biochemistry Flashcards
What are biochemicals
- organic compounds from a biological source–NO PLASTICS
- tend to be a bit larger and more complex than other organic compounds.
- 4 major types: proteins, carbohydrates, lipids, nucleic acids
4 major types of biochemicals
- proteins: made of amino acids
- Carbohydrates: made of monosaccharides (simple sugars)
- lipids: made of fatty acids
- Nucleic acids: sugar phosphates and organic bases
*the building blocks or units of each biochemical are called polymers
Polymers
- “mer” means “thing” in greek
- the building blocks of each biochemical i.e. amino acids, monosaccharides, fatty acids, sugar-phosphates+bases
- the building blocks combine to produce polymers
- the basic unit =monomer
- 2 together=dimer
- 3together=trimer
- 4-15 together=oligomers
- 15+ together =polymers
3 types of biochemical reactions
- decomposition rxn
- ex. catabolic rxn. often happens in our stomach and intestines when we eat. break down molecules
- synthesis rxn
- happens at the cellular level. form more complex molecules
- exchange rxn
- happen at cellular level. require very little energy. like breaking down glucose. molecule just gets changed a little. AB+CD= AC and BD
Monosaccharides
-carbohydrates
-they form lactone rings which contain carbon and one oxygen
-hexoses–6-carbon
sugars
-glucose–primary source of body’s energy
-fructose–fruits and veggies
-galactose–from dairy products
-pentoses–5-carbon sugars
-ribose and deoxyribose–these are found in our genetic material. not used for energy
-all taste sweet
-fuel our metabolism
carbohydrates
- carbo=carbon
- hydrate= H2O aka hydrogen and oxygen
- normally composed of C, H, O in the ratio of C1H2O1.
- contain several -OH groups (hydroxyl groups are functional side groups) the molecules are generally polar and hydrophilic
- main role in body is fuel! through catabolic and redox rxns the energy stored in carbohydrates is released and used for cellular processes
- the monomer= monosaccharide
disaccharides
- molecule with two monosaccharides joined by a polar covalent bond
- formed by dehydration synthesis–a hydrogen atom is removed from fructose and a hydroxyl group is removed from glucose and a molecule of water is formed and the two monosaccharides now share an oxygen left by the hydrogen atom.
- can be broken down by hydrolysis–the reverse process of dehydration synthesis.
- 2 most common disaccharides:
1. sucrose–(glucose +fructose) table sugar
2. lactose (glucose+galactose) milk and other dairy.
polysaccharides
- largest and therefore, least soluble
- long branching chains of monosaccharides joined by covalent bonds formed by dehydration synthesis.
- plants and animals store their glucose for later use in the form of polysaccharides
- plant glucose stored as starch, animal glucose as glycogen–found primarily in liver and skeletal muscles. - glycogen is branched and this is an advantage as enzymatic reactions happen only on the ends of molecules but there are many ends so the blood glucose concentration can increase quickly when needed. but energy stores get used up quickly as well.
- sometimes attach to lipids and proteins==glycolipids and glycoproteins (responsible for cell recognition and structural integrity of cell)
hydrocarbons
- all combos of hydrogen adn carbon
- as carbon increases by 1, hydrogen increases by 2 starting at CH4 (methane)
- their physical properties at room temperature (gas-solid-liquid-oil-etc) change as their size increases
- all are combustible
- but otherwise very stable so don’t undergo chemical rxns easily. need functional side groups for that.
isomers
- molecules with the same molecular formula but different structures are called isomers
- “same parts”
- ex. fructose and galactose
functional side groups
- structures that tack onto hydrocarbon back bone and change the fxn.
- these are more polar, give the hydrocarbons more polarity
- OH alcohol
- CHO aldehyde
- COOH carboxyl
- NH2 amine
- SH sulfhydryl
- R2CO ketone
proteins
- monomer=amino acids
- 21 different amino acids
- only form bonds in single chains, no branches
- most proteins are 100-200 amino acids
- main fxns:
1. fibrous proteins form scaffolding of body: skin, bone, tissues etc
2. globular proteins help maintain homeostasis
3. enzymes special proteins that acts as chemical catalysts and mediate chem rxns; decrease activation energy needed for rxn.
protein structure
- 3 types
primary: amino acid CHAIN
secondary: chain COILS and FOLDS
tertiary: coiled chain FOLDS in on itself and is stabilized by crosslinks and hydrogen bonds - the sequence of amino acids in the chain determines both secondary and tertiary structure
- there can be a quarternary structure in which the proteins interact with each other
“lock and key” mechanism for enzyme catalysis
- enzyme has active site where substrates (amino acids) can plug in.
- the enzyme changes shape to hold the amino acids in position
- energy is absorbed and a bond is formed
- water is released
- the bond has changed the shape of the substrates so they pop out as a new peptide bond.
- enzyme returns to original shape, ready to catalyze another rxn
metabolism
- sum of all chem rxns in the body
- all rxns mediated directly or indirectly by enzymes
- if you control what enzymes are available, you control metabolism
- if you control metabolism, you control life.