Shortcut Methods

1. Cell Size:

  • Typical plant cell size: 10-100 µm (micrometers)
  • Typical animal cell size: 10-30 µm (micrometers)
  • Red Blood Cell (Erythrocyte) size: Approximately 7-8 µm in diameter

2. Organelle Dimensions:

  • Mitochondria: Length 0.5-1 µm, Diameter 0.2-0.5 µm
  • Chloroplasts: Length 5-10 µm, Width 2-4 µm
  • Nucleus: Diameter 5-10 µm
  • Ribosomes: Diameter 15-20 nm (Prokaryotic) and 20-25 nm (Eukaryotic)

3. Membrane Potential:

  • Typical resting membrane potential of a cell: -70 mV to -90 mV

4. Surface Area to Volume Ratio:

For a spherical cell with radius “r”:

  • Surface Area = 4πr^2
  • Volume = (4/3)πr^3
  • Surface Area to Volume Ratio = (3/r)

5. Diffusion and Osmosis:

  • Diffusion: Movement of molecules from higher to lower concentration
  • Osmosis: Movement of water molecules across a selectively permeable membrane from a hypotonic solution (lower solute concentration) to a hypertonic solution (higher solute concentration).

Terms To Remember

  • Water Potential (Ψ): Measure of the tendency of water to move from one region to another based on solute concentration.
  • Tonicity: Describes the effect of the extracellular environment on a cell’s water balance.

6. Active Transport:

  • Sodium-Potassium Pump: Transports 3 Na+ ions out of the cell and 2 K+ ions into the cell, maintaining concentration gradients.
  • Proton Pump: Transports hydrogen ions (H+) across the thylakoid membrane during photosynthesis, creating a proton gradient.

7. Protein Structure:

  • Van der Waals Forces: Weak forces that contribute to the stabilization of protein structures.
  • Peptide Bonds: Covalent bonds formed between amino acids during protein synthesis.
  • Polypeptide Chain: Linear sequence of amino acids linked by peptide bonds.
  • Primary Structure: Sequence of amino acids.
  • Secondary Structure: Regular patterns of amino acid folding, including α-helices and β-pleated sheets.
  • Tertiary Structure: Three-dimensional structure of a single polypeptide chain.
  • Quaternary Structure: Arrangement of multiple polypeptide chains into a functional protein.

8. Enzyme Kinetics:

  • Enzyme-Substrate Complex: Temporary molecular complex formed between an enzyme and its substrate.
  • Km: Michaelis-Menten constant, represents the substrate concentration at which the enzyme reaction rate is half of its maximum velocity (Vmax).
  • Vmax: Maximum reaction rate achieved by an enzyme at saturating substrate concentration.

9. Nucleic Acids:

  • Nucleotide: Basic building block of nucleic acids, composed of a nitrogenous base, a pentose sugar, and a phosphate group.
  • Double Helix: Structural model of DNA proposed by Watson and Crick, consisting of two strands twisted around each other in a spiral shape.
  • Base Pairing: Specific hydrogen bonding between complementary nitrogenous bases (adenine with thymine and guanine with cytosine) maintains the stability of the double helix.

10. Gene Expression:

  • Transcription: Process of copying the genetic information from DNA to messenger RNA (mRNA) molecules.
  • Translation: Process of converting the genetic code in mRNA into a sequence of amino acids in proteins.
  • Genetic Code: Set of three-nucleotide sequences (codons) that specify which amino acid will be incorporated into a protein.
  • Central Dogma of Molecular Biology: Describes the two-step process of transcription and translation, which allows the information in genes to direct protein synthesis.