FOM anki flashcards week 2
What is the polarity of water?
Unequal electron sharing between hydrogen and oxygen leads to a dipole (partially positive H, partially negative O).
What structure does water have?
Water has a bent structure (tetrahedral bonding angle).
What are hydrogen bonds?
Bond between hydrogen (positive) and oxygen (negative) or other electronegative atoms. Essential for water’s properties.
How does the hydrophobic effect work?
Non-polar molecules aggregate in aqueous solutions (e.g., micelles, lipid bilayers).
Define amphipathic molecules.
Molecules with both hydrophilic and hydrophobic regions (e.g., phospholipids in cell membranes).
What is the primary function of cell membranes?
Selective barrier to the external environment, involved in signaling, transport, and recognition.
What is the basic structure of amino acids?
Alpha carbon bonded to amino group (-NH₂), carboxyl group (-COOH), hydrogen, and R group (side chain).
Classify amino acids.
Non-polar (hydrophobic), Polar (hydrophilic), Acidic (negative charge), Basic (positive charge).
How are peptide bonds formed?
Peptide bonds form through dehydration between amino acids, with partial double bond character.
Define protein primary structure.
Linear sequence of amino acids forming a polypeptide chain.
Describe the secondary structure of proteins.
Local folding of polypeptide backbone (alpha helix, beta-sheet, triple helix).
How is tertiary structure stabilized?
By hydrogen bonds, disulfide bridges, ionic interactions, and hydrophobic interactions.
What causes protein denaturation?
Disruption of secondary, tertiary, and quaternary structures due to heat, pH extremes, or chemicals.
Describe the quaternary structure of proteins.
Arrangement of multiple polypeptide subunits into a functional protein (e.g., hemoglobin).
What is the role of enzymes?
Biological catalysts that lower activation energy and increase the rate of biochemical reactions.
Describe Michaelis-Menten kinetics.
Relates reaction rate to substrate concentration, with Km (half-maximal velocity) and Vmax (maximum rate).
What are the types of enzyme inhibition?
Competitive, non-competitive, and uncompetitive inhibition.