Across
- 1. Tetrameric oxygen-transport protein that exhibits cooperative binding.
- 5. Pancreatic protease that cleaves peptide bonds within protein chains.
- 6. Enzyme that removes amino acids from the C-terminal end of peptides.
- 7. Molecule containing both positively and negatively charged functional groups.
- 9. Neurodegenerative disease associated with alpha-synuclein aggregation and Lewy bodies.
- 11. Severe nutritional deficiency characterized by marked wasting and loss of body fat.
- 12. Process in which genetic information in DNA is copied into messenger RNA.
- 16. Neurodegenerative disease associated with amyloid-beta plaques and tau tangles.
- 17. Level of protein structure characterized by alpha helices and beta sheets.
- 18. Nonpolar branched-chain amino acid that replaces glutamate in sickle hemoglobin.
- 20. Enzyme that removes amino acids from the N-terminal end of peptides.
- 25. Only standard amino acid without a chiral alpha carbon.
- 27. Inherited blood disorder caused by reduced synthesis of alpha or beta globin chains.
- 28. Essential branched-chain amino acid represented by the one-letter code L.
- 29. Polar amino acid with a hydroxyl group that can undergo phosphorylation.
- 32. Cyclic amino acid that restricts backbone flexibility and introduces turns.
- 33. Disruption of higher-order protein structure without usually breaking peptide bonds.
- 34. Sulfur-containing amino acid that forms disulfide bonds between protein regions.
- 37. Inactive enzyme precursor that helps prevent pancreatic autodigestion.
- 38. Intestinal epithelial cell responsible for absorbing amino acids and small peptides.
- 40. Protein-energy malnutrition characterized by edema and fatty liver.
- 41. Chemical reaction that forms a peptide bond with the release of water.
- 43. Level of protein structure involving the association of multiple polypeptide subunits.
- 45. Monomeric muscle protein that stores oxygen and lacks cooperative binding.
- 46. Intestinal cell membrane surface facing the intestinal lumen.
- 47. Amino acid containing an imidazole ring that can accept or donate protons near physiological pH.
- 48. Overall three-dimensional folding of a single polypeptide chain.
Down
- 2. Brush-border enzyme that converts trypsinogen into its active form.
- 3. Aromatic amino acid containing an indole ring that contributes to ultraviolet absorption.
- 4. Proton-linked intestinal transporter responsible for dipeptide and tripeptide uptake.
- 8. Intestinal cell membrane surface through which amino acids enter portal circulation.
- 10. Level of protein structure defined by the linear order of amino acids.
- 13. Genetic disorder in which defective CFTR function causes thick mucus secretions.
- 14. Aromatic amino acid containing a phenolic hydroxyl group involved in phosphorylation.
- 15. Cellular complex that degrades proteins marked for selective destruction.
- 19. Essential branched-chain amino acid represented by the one-letter code I.
- 21. Small protein that tags selected intracellular proteins for degradation.
- 22. Essential sulfur-containing amino acid with a thioether side chain.
- 23. Organelle containing hydrolytic enzymes that degrade cellular material.
- 24. Negatively charged amino acid replaced by valine at position six of the beta-globin chain in sickle cell disease.
- 26. Inherited neutral amino acid transport disorder that may cause pellagra-like symptoms.
- 30. Specific N-to-C arrangement of amino acids that determines peptide identity.
- 31. Process in which ribosomes use messenger RNA to synthesize a polypeptide.
- 32. Gastric enzyme that begins dietary protein digestion in the stomach.
- 34. Pancreatic endopeptidase that breaks internal peptide bonds.
- 35. Inherited renal transport disorder associated with cystine kidney stones.
- 36. Cellular process that delivers damaged organelles and protein aggregates for recycling.
- 39. Pancreatic enzyme that activates several other digestive enzyme precursors.
- 42. Protein that assists proper folding and helps prevent aggregation of new polypeptides.
- 44. Misfolded infectious protein capable of inducing abnormal folding in other proteins.