biology a level
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biology a level - Leaderboard
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105 questions
| 🇬🇧 | 🇬🇧 |
| Function of smooth/rough endoplasmic reticulum | Smooth: lipid, steroid synthesis rough: protein synthesis |
| NA | NA |
| Visual difference between smooth endoplasmic reticulum and Golgi apparatus | SER has connections, Golgi does not Golgi also has Golgi vesicles coming out |
| Structure of collagen, why is it water resistant, and what bonds make it up | Primary, secondary and quaternary structure. 3 secondary structures twist together to form a triple helix. Every third amino acid is glycine (smallest amino acid) to make the structure tight. There is no tertiary structure so that collagen does not dissolve in water. Weak hydrogen bonds and covalent bonds |
| Structure of collagen, why is it water resistant, and what bonds make it up | Primary, secondary and quaternary structure. 3 secondary structures twist together to form a triple helix. Every third amino acid is glycine (smallest amino acid) to make the structure tight. There is no tertiary structure so that collagen does not dissolve in water. Weak hydrogen bonds and covalent bonds |
| Define lysosomes | Contains hydrolytic enzymes to digest unwanted organelles or whole cells when they die |
| What are transmembrane proteins | Intrinsic/integral proteins that span the whole phospholipid bilayer |
| Visual difference between smooth endoplasmic reticulum and Golgi apparatus | SER has connections, Golgi does not Golgi also has Golgi vesicles coming out |
| Visual difference between smooth endoplasmic reticulum and Golgi apparatus | SER has connections, Golgi does not Golgi also has Golgi vesicles coming out |
| Visual difference between smooth endoplasmic reticulum and Golgi apparatus | SER has connections, Golgi does not Golgi also has Golgi vesicles coming out |
| Visual difference between smooth endoplasmic reticulum and Golgi apparatus | SER has connections, Golgi does not Golgi also has Golgi vesicles coming out |
| Visual difference between smooth endoplasmic reticulum and Golgi apparatus | SER has connections, Golgi does not Golgi also has Golgi vesicles coming out |
| Visual difference between smooth endoplasmic reticulum and Golgi apparatus | SER has connections, Golgi does not Golgi also has Golgi vesicles coming out |
| Visual difference between smooth endoplasmic reticulum and Golgi apparatus | SER has connections, Golgi does not Golgi also has Golgi vesicles coming out |
| Quaternary structure | 2 or more polypeptide chains each having a tertiary structure bonded together |
| Quaternary structure | 2 or more polypeptide chains each having a tertiary structure bonded together |
| Quaternary structure | 2 or more polypeptide chains each having a tertiary structure bonded together |
| Quaternary structure | 2 or more polypeptide chains each having a tertiary structure bonded together |
| Quaternary structure | 2 or more polypeptide chains each having a tertiary structure bonded together |
| Quaternary structure | 2 or more polypeptide chains each having a tertiary structure bonded together |
| Quaternary structure | 2 or more polypeptide chains each having a tertiary structure bonded together |
| Structure of collagen, why is it water resistant, and what bonds make it up | Primary, secondary and quaternary structure. 3 secondary structures twist together to form a triple helix. Every third amino acid is glycine (smallest amino acid) to make the structure tight. There is no tertiary structure so that collagen does not dissolve in water. Weak hydrogen bonds and covalent bonds |
| Structure of collagen, why is it water resistant, and what bonds make it up | Primary, secondary and quaternary structure. 3 secondary structures twist together to form a triple helix. Every third amino acid is glycine (smallest amino acid) to make the structure tight. There is no tertiary structure so that collagen does not dissolve in water. Weak hydrogen bonds and covalent bonds |
| Structure of collagen, why is it water resistant, and what bonds make it up | Primary, secondary and quaternary structure. 3 secondary structures twist together to form a triple helix. Every third amino acid is glycine (smallest amino acid) to make the structure tight. There is no tertiary structure so that collagen does not dissolve in water. Weak hydrogen bonds and covalent bonds |
| Structure of collagen, why is it water resistant, and what bonds make it up | Primary, secondary and quaternary structure. 3 secondary structures twist together to form a triple helix. Every third amino acid is glycine (smallest amino acid) to make the structure tight. There is no tertiary structure so that collagen does not dissolve in water. Weak hydrogen bonds and covalent bonds |
| Structure of collagen, why is it water resistant, and what bonds make it up | Primary, secondary and quaternary structure. 3 secondary structures twist together to form a triple helix. Every third amino acid is glycine (smallest amino acid) to make the structure tight. There is no tertiary structure so that collagen does not dissolve in water. Weak hydrogen bonds and covalent bonds |
| Define mitochondria | Site of aerobic respiration, where most of the ATP is released |
| What are transmembrane proteins | Intrinsic/integral proteins that span the whole phospholipid bilayer |
| Visual difference between smooth endoplasmic reticulum and Golgi apparatus | SER has connections, Golgi does not Golgi also has Golgi vesicles coming out |
| Structure of collagen, why is it water resistant, and what bonds make it up | Primary, secondary and quaternary structure. 3 secondary structures twist together to form a triple helix. Every third amino acid is glycine (smallest amino acid) to make the structure tight. There is no tertiary structure so that collagen does not dissolve in water. Weak hydrogen bonds and covalent bonds |
| Structure of collagen, why is it water resistant, and what bonds make it up | Primary, secondary and quaternary structure. 3 secondary structures twist together to form a triple helix. Every third amino acid is glycine (smallest amino acid) to make the structure tight. There is no tertiary structure so that collagen does not dissolve in water. Weak hydrogen bonds and covalent bonds |
| Structure of collagen, why is it water resistant, and what bonds make it up | Primary, secondary and quaternary structure. 3 secondary structures twist together to form a triple helix. Every third amino acid is glycine (smallest amino acid) to make the structure tight. There is no tertiary structure so that collagen does not dissolve in water. Weak hydrogen bonds and covalent bonds |
| Permanent vacuole | Storage of water, ions, pigments, and sugars. provides turgidity to cell. pushes chloroplasts to the edge of the cell to perform photosynthesis |
| What are transmembrane proteins | Intrinsic/integral proteins that span the whole phospholipid bilayer |
| Visual difference between smooth endoplasmic reticulum and Golgi apparatus | SER has connections, Golgi does not Golgi also has Golgi vesicles coming out |
| Chloroplast | Contains chlorophyll which is the site of photosynthesis. Light dependent reactions take place in the grana, producing ATP |
| Functions of nucleus | Contains Nucleolus, nuclear pore, and nuclear envelope contains DNA/chromosomes, which Control protein synthesis Transcription of Genes / production of mRNA |
| NA | NA |
| Why is DNA contained in the nucleus | Protected from degradation |
| What does nucleolus do | Manufactures ribosomal RNA and make subunits of ribosomes |
| What is nuclear pore | Passage of large molecules such as mRNA out of the nucleus |
| Antigens | Cell markers to let other cells know that this cell belongs in the body |
| Visual difference between smooth endoplasmic reticulum and Golgi apparatus | SER has connections, Golgi does not Golgi also has Golgi vesicles coming out |
| Active transport | Movement of particles against the concentration gradient (low to high), requires ATP as well as Transport/carrier proteins |
| Quaternary structure | 2 or more polypeptide chains each having a tertiary structure bonded together |
| Difference between bonding of tertiary and quaternary structure | Teritiary- R groups of the same polypeptide chain Quaternary- R groups of different polypeptide chains |
| Difference between bonding of tertiary and quaternary structure | Teritiary- R groups of the same polypeptide chain Quaternary- R groups of different polypeptide chains |
| Structure of collagen, why is it water resistant, and what bonds make it up | Primary, secondary and quaternary structure. 3 secondary structures twist together to form a triple helix. Every third amino acid is glycine (smallest amino acid) to make the structure tight. There is no tertiary structure so that collagen does not dissolve in water. Weak hydrogen bonds and covalent bonds. Staggered ends. |
| Difference between bonding of tertiary and quaternary structure | Teritiary- R groups of the same polypeptide chain Quaternary- R groups of different polypeptide chains |
| What type of structure do all proteins have | Primary and secondary |
| Fibrous proteins | Primary and secondary structure only, no tertiary insoluble in water eg, keratin and collagen |
| Globular proteins | Primary secondary and tertiary structure, some quaternary structure soluble in water - carried in water eg. Hemoglobin, enzymes, antibodies, insulin most proteins are globular |
| Primary structure protein | Order/sequence of amino acids in a polypeptide |
| Tertiary structure | Folded secondary structures in between R groups. Contains Weak hydrogen bonds, ionic bonds, covalent bonds, disulphide (cysteine only), hydrophobic interactions, and hydrophilic interactions. can make proteins specific shapes |
| Secondary structure protein | Alpha helix and Beta sheets held together by weak hydrogen bonds between the hydrogen of the carboxyl group and the oxygen of the amine group |
| Quaternary structure | 2 or more polypeptide chains each having a tertiary structure bonded together |
| Prosthetic group | Extra thing added to protein to make it function better |
| Where can disulsphide bridges form | In between two cysteines, which are the only amino acids that contain carbon |
| What causes globular proteins to be soluble | Hydrophilic/polar |
| What type of bond is peptide bond | Covalent bond |
| Difference between bonding of tertiary and quaternary structure | Teritiary- R groups of the same polypeptide chain Quaternary- R groups of different polypeptide chains |
| Structure of collagen | Primary, secondary and quaternary structure. 3 secondary structures twist together to form a triple helix. Every third amino acid is glycine (smallest amino acid) to make the structure tight. |
| Why is collagen water resistant | There is no tertiary structure so that collagen does not dissolve in water. |
| What do enzymes do that speed up rate of reaction | Lower activation energy to form/break bond |
| Induced fit hypothesis | Active site can change shape a little to become a complementary fit |
| What bonds make up collagen | Weak hydrogen bonds and covalent bonds |
| Define high specific heat capacity | Takes a lot of heat energy to increase the temperature by 1 degree Celsius |
| Why is high heat specific capacity make water useful in an organism | Takes a lot of energy for water to go up 1degree celsius. Therefore water will stay at the same temperature in the body, so enzymes don't denature. |
| What is high latent heat of vaporization | Takes a lot of heat energy to change liquid to gas |
| Dfine Dipol structure | Two weak poles (Water for example has Positive hydrogens and negative oxygens) |
| What temperature is water at its highest density | 4 degrees Celsius |
| Why is water good as an aid to cooling animals | High latent heat of vaoporisation |
| Ester bond | Covanlent bond. result of condensation reaction between fatty acid and glycerol |
| Unsaturated fats | Unsaturated fats have double bonds between carbons, called kinks, increasing the distance between fatty acids |
| How is sucrose formed | Glucose and fructose 1-4 glycosidic bond |
| Structure of starch | Amylose with amylopectin chains |
| Amylose | Straight chain of alpha glucose made up of 1-4 glycosidic bonds |
| Amylopectin | Branched chains of alpha glucose made up of 1-4 and 1-6 glycosidic bonds |
| Cellulose molecule | Alternating straight chain of Beta Glucose, 1-4 glycosidic link |
| Cellulose cell wall structure | Parallel cellulose molecules held together with many weak hydrogen bonds, forming microfibrils. many Microfibrils arranged in a grid pattern held together with weak hydrogen bonds to form cellulose fibers. |
| Example of disaccharides | Sucrose, maltose |
| Active transport | Movement of particles against the concentration gradient (low to high), requires ATP as well as Transport/carrier proteins |
| What are transmembrane proteins | Intrinsic/integral proteins that span the whole phospholipid bilayer |
| What can phospholipids form | Micelle - sphere Bilayer Lysosome - sphere within sphere, con contain substances inside |
| Fluid mosaic model | Fluid- Phospholipid and protein molecules can move around in the bilayer Mosaic- Different protein molecules are scattered |
| What is the middle bit of phospholipid bilayer called | Hydrophobic core |
| How to differentiate between glycoprotein and glycolipid | Proteins are connected to a protein, and glycolipid is connected to phospholipid |
| Role of cholesterol in phospholipid bilayer | Controls fluidity |
| Extrinsic proteins in phospholipid bilayer | Peripheral protein Inner or outer surface Can be bound to intrinsic proteins, phospholipids, and molecules on the inside/outside of the cell |
| What are proteins embedded into phospholipid bilayer called | Intrinsic/intergral protein, can be inside or outside. can span the whole membrane, called transmembrane proteins |
| Carrier proteins | They can change shape of the molecule to allow it to diffuse out the other way |
| What are transmembrane proteins | Intrinsic/integral proteins that span the whole phospholipid bilayer |
| Conformational change | When the molecule changes shape inside of a binding site of a carrier protein |
| Max magnifiaction of Electron microscope | Mag: 250,000x (2,000 times the magnification of light mircoscope) |