Prevalence: Over 7 million U.S. children diagnosed; significant portion (23%) are 17-year-old boys.
Diagnostic Complexity: Understanding of A.D.H.D. is less clear today than before; reliance on genetic or brain-based biomarkers has largely not yielded results.
Symptoms: Varied and overlap with conditions like anxiety, trauma, and autism; only 1 in 9 show consistent symptoms throughout childhood.
Temporary vs. Lifelong: Some researchers argue it may be a temporary condition rather than a lifelong disorder.
Medication Shortcomings:
Drugs like Ritalin improve symptoms in the short term (within 36 months).
Medication may enhance focus but does not guarantee better academic performance.
Affect motivation by making tasks more engaging rather than enhancing intelligence.
Environmental Influence: Children's behavior improves in supportive, engaging environments.
Evolving Perspective: Shift from a strictly medical model to one considering ADHD as a mismatch between a child's brain and their environment.
Nucleus: Site of DNA.
Cytoplasm: Where translation occurs.
mRNA (messenger RNA): Carries genetic information from DNA.
tRNA (transfer RNA): Brings amino acids to the ribosome.
Ribosome: Site of protein synthesis that translates mRNA into a polypeptide chain.
Codon Recognition: tRNA pairs with the corresponding mRNA codon.
Peptide Bond Formation: Amino acids on adjacent tRNAs form a peptide bond.
Translocation: Ribosome moves the tRNA from the A site to the P site, advancing the mRNA in the ribosome.
Release Factor: Binds to the stop codon on mRNA, facilitating hydrolysis between last amino acid and tRNA.
Post-Termination: Disassembly of ribosomal subunits and degradation of mRNA to be recycled.
Stop Codons: UAG, UAA, and UGA are three stop codons used in translation.
Total of 64 mRNA codons but only 61 coding (3 are stop codons).
There are about 40 tRNA molecules for codon recognition.
Wobble base pairing: Some tRNAs can pair with multiple codons due to flexibility in the third base of the codon, following specific rules.
Protein Structure Levels:
Primary Structure: Linear chain of amino acids (e.g. A1, A2)
Secondary Structure: Formation of shapes like alpha-helices or pleated sheets.
Tertiary Structure: Overall 3D structure of a single protein (e.g. Hemoglobin).
Quaternary Structure: Association of multiple protein subunits.
Post-Translational Modifications:
Phosphorylation: Common modification that regulates protein activity.
Glycosylation: Tags proteins to promote folding and stability.
Methylation: Affects transcription regulation, RNA processing, and other cellular processes.