Across
- 3. A protein is compact, generally water-soluble, and has hydrophilic R-groups exposed to its surroundings. It belongs to this structural classification. (G)
- 8. A functional protein contains four folded polypeptide chains assembled together. Their three-dimensional arrangement represents this level of structure. (Q)
- 9. A compact, soluble protein binds to specific receptors on target cells and triggers signalling that promotes glucose uptake. Identify the protein. (I)
- 10. A protein contains four polypeptide subunits, each associated with an iron-containing haem group. Identify the protein. (H)
- 13. A protein contains multiple polypeptide chains but no non-protein component. It belongs to this classification. (N)
- 16. A mutation changes interactions between R-groups, altering the overall folding of a single polypeptide. This level of structure is affected. (T)
- 17. Heating a protein disrupts interactions maintaining its three-dimensional shape, causing it to lose its normal function. This process has occurred. (D)
- 19. Two amino acid R-groups carry opposite electrical charges and are positioned close together. This type of bond may form between them. (I)
- 22. A mutation changes the order of amino acids in a polypeptide. This level of protein structure is directly altered. (P)
- 23. The arrangement of hydrophobic and hydrophilic R-groups in a protein depends partly on the chemical properties of the R-groups and the surrounding ________. (E)
- 27. A student claims that alpha helices are stabilized by interactions between R-groups. In fact, this type of bond forms between groups in the polypeptide backbone. (H)
- 28. A protein consists of three polypeptide chains arranged in a triple helix, forming strong fibres that resist pulling forces. Identify the protein. (C)
- 31. Two amino acids have identical backbone structures but different chemical properties. The difference is due to this variable component. (R)
- 32. A protein contains a covalent bridge between two sulfur-containing R-groups. Both amino acids involved must be this type. (C)
- 33. Two cysteine residues become positioned close together during protein folding. Their sulfur atoms may form this type of covalent bridge. (D)
- 34. A mutation replaces a nonpolar amino acid with a charged amino acid in the core of a soluble protein. This type of interaction may be disrupted. (H)
Down
- 1. A functional protein contains multiple polypeptide chains. Each individual chain is called a ________. (S)
- 2. A change in DNA alters an amino acid in a polypeptide, potentially affecting its folding and function. This genetic change is called a ________. (M)
- 4. Hydrogen bonds form between neighbouring sections of a polypeptide backbone arranged side by side. This secondary structure results. (B)
- 5. An R-group loses a hydrogen ion and becomes negatively charged. It belongs to this category. (A)
- 6. Hydrogen bonds form between backbone C=O and N-H groups of amino acids four positions apart, stabilizing this secondary structure. (A)
- 7. An amino acid R-group is exposed on the surface of a soluble protein and interacts favourably with water. It has this property. (H)
- 11. Two polypeptides have identical amino acid sequences and fold under the same conditions. They would generally adopt the same characteristic three-dimensional shape, called their ________. (C)
- 12. Haemoglobin contains a haem group associated with each polypeptide subunit. The haem is an example of this type of non-protein component. (P)
- 14. Scientists rapidly freeze protein samples and use electrons to investigate their three-dimensional structures. This imaging technique is abbreviated as ________. (C)
- 15. An R-group forms hydrogen bonds with water but carries no overall electrical charge. It is classified as this. (P)
- 18. A polypeptide is broken down completely by hydrolysis. These are the monomers that would be released. (A)
- 20. A protein contains a haem group in addition to its polypeptide chains. It belongs to this classification. (C)
- 21. An amino acid is found buried in the core of a water-soluble globular protein. Its R-group is most likely classified as this. (N)
- 24. The type of covalent bond broken when a polypeptide undergoes complete hydrolysis. (P)
- 25. An R-group accepts a hydrogen ion and becomes positively charged. It belongs to this category. (B)
- 26. A protein contains regions of regular coiling and pleating stabilized by backbone hydrogen bonds. These regions represent this level of structure. (S)
- 29. A membrane protein contains hydrophobic regions exposed to the fatty acid tails of phospholipids. This describes an ________ membrane protein. (I)
- 30. A protein has an elongated shape and forms strong structures that provide support and resist pulling forces. It belongs to this structural classification. (F)