Lecture Title: BIOCH-521 - Lecture 1
Focus: Introduction & Aqueous Solutions
Key Question: What is biochemistry?
Biochemistry occurs primarily in aqueous solutions, emphasizing the significance of water.
Lecture Topics to Cover:
Weak interactions between molecules, which are fundamental to all biochemical processes.
Biochemistry is the study of chemical processes in living organisms.
It encompasses the interactions between:
Organisms and their ecosystems
Atoms and molecules
Cells and organs
Examples:
Sickle Cell disease
ATD toxin produced by pufferfish hemoglobin
Proteins
Composed of polymers of amino acids folded into specific 3D structures.
Functions include catalyzing reactions (enzymes), providing structural support, signaling, and mobility.
Nucleic Acids
DNA and RNA are polymers of nucleotides, pivotal for storing and conveying genetic information.
Also involved in energy metabolism (e.g., ATP).
Lipids
Comprise hydrophobic hydrocarbons linked to hydrophilic head groups.
Functions include cellular membrane formation, energy storage, and cell signaling.
Carbohydrates
Formed from carbon hydrates (CH2O)n and can create large polymers.
Roles include energy storage, structural functions, and serving as components of proteins, nucleic acids, and lipids.
The Central Dogma (Francis Crick, 1958) explains cellular information processing.
The flow of information follows the pathway:
DNA -> RNA -> Protein
Cell Signaling (Signal Transduction)
Refers to how physiological stimuli are received by cells, resulting in varied cellular responses.
Metabolism
Encompasses chemical reactions that generate energy and produce biomolecule building blocks.
Essential for sustaining life.
Biochemistry focuses on chemical processes vital for life.
Four Major Classes of Biochemical Molecules:
Proteins, Nucleic Acids, Lipids, Carbohydrates
Understanding the Central Dogma is fundamental: DNA -> RNA -> Protein
Properties of Water:
Water is polar; oxygen carries a slight negative charge (δ-), while hydrogens have a slight positive charge (δ+).
Facilitates the formation of hydrogen bonds leading to:
Cohesion among water molecules
Solubility of polar biomolecules
Hydrophobic Effect
Non-polar molecules aggregate in water, driven by increased entropy.
Higher disorder results from hydrophobic molecules clustering together, a vital process for biological systems.
The hydrophobic effect intuitively drives two processes:
Protein Folding: Organizing from unstructured to structured states.
Membrane Formation: Hydrophilic heads orient towards the water while hydrophobic tails gather inward.
Electrostatic Interactions
Occur between distinctly charged molecules and can be weakened by the presence of water.
Example: Salt bridges commonly found in proteins.
Hydrogen Bonds (H-bonds)
Non-covalent interactions essential for the stability of structures like the DNA double helix and proteins.
Typically occur between hydrogen and electronegative atoms (e.g., O, N).
Van der Waals Interactions
Weak interactions based on transient charge distributions, stabilizing molecules when closely packed.
They are crucial despite being relatively weak compared to other forces.
Four Essential Interactions in Biomolecules
Electrostatic – 40-200 kJ/mol
Hydrogen Bonds – 4-13 kJ/mol
Hydrophobic – 3-10 kJ/mol
Van der Waals – 2-4 kJ/mol
Covalent Bonds: significantly stronger (200-400 kJ/mol).
Biochemical interactions predominantly occur in aqueous environments characterized by H-bonds.
The hydrophobic effect is crucial, emphasizing entropy-driven processes in biology.
Weak interactions (electrostatic, H-bonding, Van der Waals) are integral to biochemical stability.
Contact Information: For further inquiries, reach out to dmeekins@ksu.edu.