BSC2010 Lecture 13 Review
Practice Questions
Question: Which of the following amino acids is not commonly phosphorylated?
A. Tyrosine
B. Serine
C. Cysteine
D. Threonine
Allosteric Regulation of Enzyme Activity
Allosteric sites can be modified by:
Reversible covalent binding of a molecule
Phosphorylation: A phosphate group is added by a protein kinase on an amino acid residue (serine, threonine, or tyrosine).
If the modification occurs in a hydrophobic region, it may induce changes that affect interactions with hydrophilic regions of the enzyme.
Protein Phosphatases: Remove phosphate groups from proteins.
Significance of Phosphorylation: It is crucial for cells to regulate enzymes and other proteins.
R Group Modification Through Phosphorylation
Phosphorylated Amino Acids:
Serine: Phosphoserine
Threonine: Phosphothreonine
Tyrosine: Phosphotyrosine
Impact of R Group Modification:
The addition of a chemical group changes interactions with nearby amino acids, affecting the protein's shape.
The Twenty Common Amino Acids
Grouped according to properties conferred by their side chains:
Differences in charge, polarity, size, shape, and functional groups lead to structural diversity and specificity in interactions.
Examples of Amino Acids:
Glycine: Small, fits into tight corners.
Proline: Forms a covalent bond with its hydrocarbon side chain causing a ring structure, which stabilizes bends or loops in proteins.
Formation of Disulfide Bonds
Cysteine:
Contains a terminal sulfhydryl (─SH) group that can react with another cysteine side chain to form a disulfide bridge or disulfide bond (─S─S─).
Function: Stabilization of the three-dimensional structure of proteins.
Primary Active Transport
Definition: Involves the direct hydrolysis of ATP for energy.
Sodium-Potassium Pump (Na+-K+ Pump):
Moves Na+ out of a cell while bringing K+ in.
For every molecule of ATP consumed, 3 Na+ ions are pumped out, and 2 K+ ions are pumped in, maintaining concentration gradients.
Differences Between Active and Passive Transport
Active Transport: Requires energy input, moves substances against their concentration gradients via carrier proteins.
Passive Transport: Does not require energy, substances move down their concentration gradients.
Signal Transduction and Cellular Response
Concept Overview:
Cells can detect and respond to signals through specific receptors.
Signals can promote various cellular responses such as opening ion channels or altering enzyme activity.
Signal Amplification
The cascade of cellular events during signal transduction increases the amplification and distribution of the initial signal.
Cellular Respiration
Inputs for Cellular Respiration:
Glucose and oxygen are the main inputs.
ATP Production: A single glucose molecule can yield approximately 30 to 32 ATP during aerobic respiration, involving glycolysis, pyruvate oxidation, the citric acid cycle, and oxidative phosphorylation:
Glycolysis: Glucose → 2 pyruvate + 2 ATP + 2 NADH
Pyruvate Oxidation: 2 Pyruvate → 2 CO₂ + 2 Acetyl CoA + 2 NADH
Citric Acid Cycle: 2 Acetyl CoA → 4 CO₂ + 2 GTP + 6 NADH + 2 FADH₂
Oxidative Phosphorylation: 10 NADH + 2 FADH₂ → approximately 26-28 ATP
Photosynthesis Overview
Two main pathways involved:
Light Reactions: Convert light energy into chemical energy (ATP and NADPH).
Carbon Fixation Reactions: Use ATP and NADPH to produce carbohydrates.
Practice Questions Summary
Carbon dioxide is:
a) nonpolar; simple diffusion
b) polar; facilitated diffusion
During a typical hydrolysis reaction:
Energy required for bond breaking vs. energy released during product formation.
Enzyme Functionality:
Enzymes lower activation energy and regulate cell activity.
Conclusion
Understanding the properties and functions of biomolecules is core to cellular biology, driving processes such as signal transduction, energy metabolism, and the structural roles of proteins.