Biochem Flashcards
What kind of bonding is shown in the phospholipid bilayer
Hydrophobic forces between long hydrophobic chains in midlayer
What is acylation
Addition of a group containing a carbon double bonded to oxidation
What type of reaction is condensation
Anabolic (2 smaller molecules are ‘built up’ to a larger molecule)
What type of reaction is hydrolysis
Catabolic (larger molecule broken down)
What is the final oxidative stage of carbon
Carbon dioxide
What is metabolism
Net oxidative process where carbon is fully reduced to an oxidised state
Functions of biomolecules
Information storage
Structural
Energy generation
Energy/currency storage - atp
Communication - receptors, hormones etc
What are the classes of biomolecules
Peptides and proteins
Lipids
Nucleic acids
Carbohydrates - saccharides
How is energy stored within the cell
Through carbohydrates in the form of carbon chains
What makes the glucose molecules a reducible target
The oxygen atom between carbon 1 and carbon 5
How are disaccharides formed
Covalent bonds between c1 - c4 or c1-c2
What is polymeric glucose
Glycogen - energy store
Which carbon links form the polymer, glycogen?
C1-c6
When is some energy unavailable to do work
When energy is transformed
What is an exergonic reaction
If the free energy change is negative
When can reactions occur spontaneously
If the change in free energy is negative
What are examples of exergonic reactions
Energy left over from reaction can do work such as conversion of glycogen to glucose
What are endergonic reactions
Free energy change is positive
Cannot occur spontaneously - need an input of energy
What shape is a water molecule
Tetrahedral (lone pairs)
What substances are hydrophilic
Ionic and polar (can dissolve in water)
What is the isoelectric point of a molecule
The pH at which a molecule has no net charge
How many pKa values do amino acids with no charge have
2 as they have 2 titratable groups
How can proteins act as buffers
Several amino acid side chains can be ionised
What happens to a protein if there is a change in pH
Can change ionisation of a protein which can lead to a change in structure therefore function
How is hydrogen bonding promoted in biomolecules
Difference of EN of atoms in water create dipoles
How can amphipathic molecules span polar and non-polar environments
Due to hydrophobic and hydrophilic domains
Where do the unique buffering abilities of protein come from
Zwitterionic properties of amino acids
How can changes in protein conformation arise
Redox interaction that affect the state of metal ion centres
Disulphide bridges
Salt bridging
Hydrophobic interactions
Electrostatic (polar?) interactions
What strutcure of the protein is important to its function
Tertiary (peptide fold)
What can changes in amino acid sequence lead to
Altering of function
