Proteins: Most abundant and functionally diverse biomolecules in the body.
Glutamine Stretch: Related to misfolded proteins often seen in Alzheimer’s disease.
Sickle Cell Anemia: Amino acid substitution where glutamic acid is replaced by valine at position #6.
Respiratory Acidosis: Caused by hyperventilation due to retention of CO2.
Isoelectric Point: The pH at which an amino acid has no net charge, important for understanding amino acid behavior in electrophoresis.
Zwitterions: Molecules with equal ionizable groups of opposite charge, commonly present in amino acids.
Michaelis-Menten Equation: Describes enzyme kinetics and how reaction rates change with substrate concentration.
Leucine & Glutamine: Not basic amino acids essential for protein synthesis.
Peptide Bonds: Bonds linking amino acids together in peptides.
Phenylisothiocyanate: Component of Edman’s reagent, used in amino acid sequencing.
Hydrogen Bonds: Stabilizing forces in structures such as alpha-helices of proteins.
Alpha-Helices: Common structural element reversing the polypeptide direction.
Prions: Abnormal, misfolded proteins associated with Creutzfeldt-Jakob disease.
Hemoglobin & Myoglobin: The two most abundant heme proteins in humans, crucial for oxygen storage and transport.
Myoglobin: Found in heart and skeletal muscles.
Hemoglobin A: Major adult hemoglobin type.
Thalassemia: A hereditary hemolytic disease resulting from imbalanced globin synthesis.
Methemoglobin: Resulting from oxidation of the heme component in hemoglobin, leading to Fe3+ state.
Collagen & Elastin: Examples of fibrous proteins.
Collagen: Most abundant protein in the human body.
Type IV: Non-fibril forming collagen.
Rich in proline and glycine.
Elastin: Provides elasticity in connective tissues, large proteins containing multiple polypeptide regions.
Ehlers-Danlos Syndrome: A group of disorders affecting connective tissues.
Oxidoreductase: Enzyme class exemplified by lactic dehydrogenase involved in amino acid and carbohydrate metabolism.
Protein Turnover: Recycling proteins back into amino acids for use in the body.
Glycine: Optically active amino acid involved in various metabolic processes.
Tyrosine: An important amino acid not containing sulfur, a precursor to neurotransmitters.
Transamination: The first step in amino acid catabolism, exchanging amino groups between amino acids and keto acids.
Celiac Disease: A malabsorption disorder affecting dietary protein metabolism.
Albinism: Caused by melanin deficiency.
Phenylketonuria: An inherited metabolic disorder where phenylalanine cannot be converted to tyrosine, leading to severe health issues.
Maple Syrup Urine Disease: Results from defective metabolism of branched-chain amino acids (valine, leucine, isoleucine).
A-DNA & B-DNA: Two forms of right-handed DNA; Z-DNA is left-handed.
Plasmids: Extrachromosomal DNA used in bacterial genetics.
Translocation: Movement of tRNA during protein synthesis.
Covalent Bonds: Formed between atoms by sharing electrons; essential in forming stable protein structures.
Glycosidic Bonds: Bonds linking carbohydrates within polysaccharides.
Isomerization: The conversion of substrates from one isomer to another, crucial in metabolic pathways.
Micelles: Disk-shaped clusters aiding in lipid absorption.
Hyperlipoproteinemia: Genetic disorders affecting lipid transport in the bloodstream.
Acetyl CoA: Major fuel for the TCA cycle; essential metabolite linking carbohydrate and lipid metabolism.
Vitamin K: Fat-soluble vitamin crucial for blood clotting, synthesized in intestinal bacteria.
Vitamin B Deficiencies: Include conditions such as pernicious anemia associated with vitamin B12 deficiency.
Macular Degeneration: Leading cause of blindness; related to aging and oxidative stress.
Xeroderma Pigmentosum: Hereditary defect preventing DNA repair, increases skin cancer risk.
Van de Bergh Reaction: Identifies bilirubin concentration in the blood.
Ninhydrin Test: Detects free amino acids by producing a yellow color.
Biuret Test: Tests for peptide bonds, indicative of proteins in solutions.
Marasmus & Kwashiorkor: Types of malnutrition with protein deficiencies leading to severe health outcomes.
Reductase Enzymes: Enzymes that add hydrogen to substrates, important in biosynthesis.
Amylase: Enzyme responsible for breaking down carbohydrates like maltose.