Biological Molecules and Enzymes Flashcards
Hydrolysis vs dehydration
Macromolecule broken into smaller molecules with addition of water = hydrolysis, dehydration is opposite and water is a byproduct
Roles of lipids
Energy storage (due to long carbon chains) Cellular organization and structure in the membrane bc they are hydrophobic Precursor for vitamins and minerals bc they can pass through cellular membranes
What is a fatty acid, Saturated vs unsaturated fatty acid
Building block for lipid compounds CHCHCHCOO-
Unsaturated has one or more carbon carbon double bonds
What are phospholipids and what are they a component of
Lipids with a phosphate making it polar at one end and non polar at the other (amphiphathic) therefore a good structural component of membranes
What do triacylglycerols do and what’s the structure
Store metabolic energy and provide thermal insulation and padding Glycerol head (CH3) and 3 fatty acid tails
What do steroids (a type of lipid) do, structure
Regulate metabolic activities ex. Vit d, hormones, cholesterol
Four ringed
The fatty acid eicosanoid and terpenes can serve as
Hormones/signalling molecules such as prostaglandins
How are carbs useful, 2 examples
Energy source
Glucose and fructose
Glycogen , starch, and cellulose are____ that differ in their
Glucose polymers with differing linkages (alpha for glycogen)
Difference between nucleotide, nucleoside, and nucleic acid
Nucleoside is pentose(5C) sugar + nitrogenous base and nucleotide is formed with addition of phosphate. Nucleotides make up nucleic acids such as DNA
Purines
Adenine and guanine
Pyrimidines
Cytosine and thymine
Uracil (RNA)
Types of bonds in DNA double helix
Phosphodiester bond between the phosphate and carbon of sugar formed via dehydration
Hydrogens bonds between nitrogenous bases (two for AT) ( 3 for CG)
What is a primary structure of a protein - what types of bonds
Sequence of amino acids
C-N-C-N
Secondary structure of a protein and the type of bonds
Beta pleated sheet of an alpha helix
Hydrogen bonds
Which structure of a protein does proline effect
Secondary therefore also tertiary
6 factors contributing to tertiary structure
- Covalent disulfide bonds between 2 cystine amino acids
- Ionic interactions between acidic and basic side chains
- Hydrogen bonds
- Van de waals forces
- Hydrophobic side chains pushed from water toward center of protein
- R group of proline
What does denatured protein mean
Examples of denaturing agents
When the native conformation of the protein is disrupted
*** rarely effects the primary structure of a protein
Ph, heat
When you see nitrogen on the mcat think
Protein
What are enzymes
Proteins that act as catalysts (lower the energy of activation)
** forward and reverse of reaction
What is Vmax, how can it be increased
Max rate of a reaction
Increase by adding more enzymes (proportional to enzyme concentration)
What is the Michaelis constant Km
How can we change it
The substrate concentration at which the reaction rate = 1/2Vmax
Inversely proportional to enzyme affinity
Can’t change with enzymes - but can be altered by certain enzyme inhibition
Some enzymes require coenzymes to function, what are some examples
Minerals
Coenzymes
Vitamins
How are enzyme reactions effected by temperature, ph and substrate concentration ** think of the graphs
Temp increase reaction rate until at some point the enzyme denatures
Optimal ph depends on the enzyme but generally neutral - optimal pH
Rate of reaction increases with substrate until max rate has been achieved
