Unit 1 - Biological Molecules Flashcards
Examples of of monomers
Monosaccarides
Amino acids
Nucleotides
Condensation reaction points
Molecules joining together
Water is formed as a byproduct
Reaction between OH’s and H
Hydrolysis
Large to small molecules
Water is required
Forms H+ and OH- ions
What are amino acids joined together by?
Peptide bonds
Examples of proteins
Insulin
Enzymes
Structural proteins (Keratin and Collagen)
Non polar amino acid points
Hydrophobic
On the inside of proteins
Polar amino acid points
Hydrophilic
Found on the outside of proteins
Electrically charged
Have a whole charge
Want to form ionic bonds
What is the primary structure
Sequential chain of amino acids joined by peptide bonds
What are the bonds found in secondary structures?
Hydrogen bonds
What are the bonds in Tertiary structure? (In order of strength)
(Covalent) Disulphide bridges
Ionic bonds
Hydrogen bonds
What are the bonds in Tertiary structure? (In order of strength)
(Covalent) Disulphide bridges
Ionic bonds
Hydrogen bonds
Bonds found in globular proteins
Ionic and hydrogen bonds
Bond found in fibrous proteins
Disulphide bonds
Fibrous protein properties
Insoluble in water
Alpha helicies or beta pleated sheets
Disulphide bonds
Structural proteins
Globular protein properties
Soluble in water
Alpha helicies and beta pleated sheets
Ionic and hydrogen bonds
Metabolic proteins
Shape: Roughly circular
Function: Physiological
Examples: Hemoglobin, enzymes, insulin
Why do substances move at different rates in chromatography?
Affinity to the stationary phase
Solubility in the solvent
Why do substances move at different rates in chromatography?
Affinity to the stationary phase
Solubility in the solvent
Enzyme definition
Biological catalysts which provide an alternative reaction pathway with a different activation energy.
Describe the structure of enzymes?
Globular proteins with a 3D tertiary structure
Hydrophilic side chains
Have an active site
Described the induced fit model
1) Enzymes and substrates have specific tertiary structures that are roughly complementary
2) Substrate goes into active site
3) Bonds form and active site bends around substrate forming and induced fit and putting strain on the bonds
4) Activation energy is therefore lowered- substrate breaks
5) Products are released
Equation for temperature coefficient
Temperature coefficient= Rare of reaction at (x+10)/ Rate of reaction at x
Describe enzyme and decreasing PH
- In a higher PH, there are (less) H+ ions
- This causes the hydrogen and ionic bonds to break in the tertiary structure
- The enzymes denature
- Substrate and active site are no longer a complementary fit
- The enzyme substrate complex can no longer be made
Describe enzyme activity and increasing temp
- Increase in the kinetic energy of substrate and enzyme
- The enzyme and substrate move faster
- Substrate and enzyme more likely to collide
- An optimym temp is reached where are there are many random collisions but the shape of the active site hasn’t changed
- Enzymes absorb so much energy that the ionic and hydrogen bonds within them break- changing the 3D tertiary structure
- The enzymes become denatured
- There is no longer a complementary fit between the substrate and active site
Describing the effect of change of substrate conc
- Initially the substrate is the limiting factor as the enzyme (active site) is in abundance
- As substrate conc increases- more substrates can bind with active sites- forming and induced fit and giving an alternative reaction pathway with a lower activation energy.
- Eventually, the substrate is no longer the limiting factor- it is enzyme conc
- Increasing substrate conc no longer increases the rate of reaction
What are carbs made out of and in what ratio are they found?
Carbon, Oxygen and Hydrogen in the ratio CH2O
General properties of sugars
Sweet Soluble in water White Crystaline All have the suffix of OSE