Translation Basics
Understand how mRNA is translated by ribosomes and tRNAs.
Explore the steps involved in mRNA translation.
Structure and Function of the Ribosome
Investigate the structure of bacterial and eukaryotic ribosomes.
Insights from Metabolic Studies
Examine how studies on inborn errors of metabolism provide insights into protein function in heredity.
Gene-Protein Relationships
Discuss how Neurospora studies led to the One-Gene: One-Enzyme hypothesis.
Genetic Variability and Protein Structure
Explore how variations in protein structure contribute to biological diversity.
Posttranslational Modifications
Understand how posttranslational modifications affect protein functionality.
Roles of Proteins
Discover the various functions of proteins within biological systems.
Translation
Biological process that polymerizes amino acids into polypeptide chains.
Requires: amino acids, mRNA, ribosomes, and tRNA.
Transfer RNA (tRNA)
Adapts genetic information from mRNA to corresponding amino acids.
Each tRNA has an anticodon complementary to mRNA codons.
Ribosomes
Composed of ribosomal RNA (rRNA) and ribosomal proteins.
Prokaryotic ribosomes: 70S; Eukaryotic ribosomes: 80S.
Initiation
Involves mRNA, ribosomal subunits, initiator tRNA, GTP, and initiation factors.
Forms the initiation complex with tRNA binding to the start codon (AUG).
Elongation
Ribosomes scan mRNA, adding amino acids to the polypeptide chain.
Catalyzed by elongation factors like EF-Tu and EF-G.
Termination
Signaled by stop codons (UAG, UAA, UGA).
Release factors stimulate polypeptide release from tRNA.
Polyribosomes
Multiple ribosomes translating one mRNA simultaneously.
Eukaryotic translation involves more factors for initiation, elongation, and termination than in bacteria.
mRNA processing involves a 5' cap and poly-A tail for stability.
The Kozak sequence enhances translation efficiency.
Proteins vs. Polypeptides
Polypeptides are amino acid chains; proteins are folded polypeptides.
Amino Acid Classification
Amino acids categorized as nonpolar, polar, positively/negatively charged based on R groups.
Peptide Bonds
Formed via dehydration reaction between amino acids; dipeptides consist of two amino acids.
Protein Structures
Levels of structures: Primary (amino acid sequence), Secondary (alpha helices and beta sheets), Tertiary (3D conformation), Quaternary (multiple polypeptide chains).
Posttranslational modifications crucial to functional capabilities of proteins, including:
Modifications of N-terminus amino acids,
Trimming polypeptides and complexing with metals.
Proteins, as the most diverse macromolecules, perform crucial functions:
Transport Proteins: Hemoglobin and myoglobin for oxygen transport.
Structural Proteins: Collagen, keratin for tissue structure.
Contractile Proteins: Actin and myosin in muscle.
Enzymatic Proteins: Catalyze biochemical reactions, essential for metabolism.