Study Notes on Biochemistry Concepts
Partial Charges and Hydrogen Bonds
Hydrogen does not form hydrogen bonds with carbon.
Full charges arise from the loss or gain of electrons, leading to ionic bonds.
Van der Waals Forces
Caused by transient charges due to electron distribution.
Occur in all molecules; stronger in polar, weaker in non-polar.
Gecko climbing example illustrates Van der Waals forces in action.
Hydrophobic Interactions
Nonpolar molecules cluster in water, leading to energy stability and increased entropy.
Separates oil and water, promoting lower energy configurations.
Amphipathic Molecules
Have both hydrophilic and hydrophobic properties; interactions lead to protein folding and cellular structures.
Functional Groups
Important functional groups: hydrocarbons, alcohols, aldehydes, ketones, carboxyls, amines, and phosphates.
Alcohols, amines, and certain groups can form hydrogen bonds.
pH and Biological Importance
pH measures hydrogen ion concentration; crucial for enzyme activity and protein folding.
Blood pH around 7.4 is vital for health.
Autoionization of Water
Water can ionize to form H+ and OH−; equilibrium is key for maintaining proper pH.
Acids and Bases
Strong acids completely ionize in water; weak acids partially ionize to form conjugate bases.
pKa is the pH at which the concentrations of acid and conjugate base are equal.
Buffer Systems
Buffers resist pH changes within certain limits; works best near pKa values.
Example: carbonic acid and bicarbonate in blood maintain pH.
Partial Charges and Hydrogen Bonds
Partial charges ( and ) are created when electrons are shared unequally between atoms with different electronegativity values.
Hydrogen bonds are a specific type of dipole-dipole interaction involving a hydrogen atom covalently bonded to a highly electronegative atom (, , or ) which is then attracted to the lone pair of another electronegative atom.
Hydrogen does not form hydrogen bonds with carbon because the electronegativity difference between them (, ) is too small to polarize the bond significantly.
Full charges arise from the complete gain or loss of electrons (), leading to ionic bonds and the formation of distinct cations and anions.
Van der Waals Forces
These represent weak, short-range intermolecular attractions caused by transient (temporary) dipoles as electron distributions fluctuate around nuclei.
They occur in all molecules, whether polar or non-polar; while weak individually, their cumulative effect in large numbers can be substantial.
Example: Geckos utilize Van der Waals forces between the millions of microscopic hairs (setae) on their feet and the molecules of a surface to walk on walls and ceilings.
Hydrophobic Interactions
Nonpolar molecules (hydrophobes) do not interact favorably with water and tend to cluster together to minimize their surface area in contact with the polar solvent.
This clustering is driven by thermodynamics, specifically an increase in global entropy (). When nonpolar molecules aggregate, fewer water molecules are forced into rigid, "orderly" cage-like structures (clathrates) around them.
This effect is responsible for the separation of oil and water and is a primary driver for energy-stable configurations in biological systems.
Amphipathic Molecules
These molecules possess both a hydrophilic (polar/charged) "head" and a hydrophobic (nonpolar) "tail."
In water, they spontaneously assemble into structures such as micelles or lipid bilayers, which form the basis of all cellular membranes.
Amphipathic interactions are critical in protein folding, as they drive hydrophobic amino acids to the interior of the protein away from water.
Functional Groups
Functional groups determine the chemical properties and reactivity of organic molecules. Key groups include:
Hydrocarbons: (methyl), which are non-polar and hydrophobic.
Alcohols: (hydroxyl), which are polar and capable of forming hydrogen bonds.
Carbonyls: Found in aldehydes () and ketones ().
Carboxyls: , which can release a proton () to act as an acid.
Amines: , which can accept a proton () to act as a base.
Phosphates: , which are highly charged and central to energy transfer molecules like ATP.
pH and Biological Importance
pH is a logarithmic scale used to specify the acidity or basicity of an aqueous solution: .
The scale typically ranges from to . Most biological processes occur near neutrality ().
Human Blood: Maintenance of blood pH around is critical; even small deviations can lead to medical emergencies as enzymes become denatured.
Autoionization of Water
Water molecules occasionally dissociate into hydrogen and hydroxide ions: .
The equilibrium constant for this reaction at is the ion product constant, .
In pure water, , resulting in a neutral of .
Acids and Bases
Strong Acids: Dissociate completely in water (e.g., ).
Weak Acids: Only partially ionize in water, establishing an equilibrium between the acid () and its conjugate base ().
pKa: This value is the negative log of the acid dissociation constant (). It represents the pH at which the concentrations of the acid and conjugate base are exactly equal ().
Buffer Systems
Buffers are solutions that resist changes in pH when small amounts of acid or base are added; they work best when the pH is close to the compound's .
The Henderson-Hasselbalch equation defines this relationship: .
Biological Buffer: The bicarbonate system () in human blood is a key physiological buffer that prevents rapid pH changes.