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LS3 - Micro Bio (L7)
Lecture 7
| Question | Answer |
|---|---|
| Protozoan Parasite - Plasmodium. Grows inside red blood cell | malaria |
| binds 4 oxygen | hemoglobin |
| Due to mutation in β-globin gene. E6V mutation. | sickle cell anemia |
| codon change from hemoglobin → sickle cell | GAA --> GTG GAG --> GTA |
| Red Blood Cell membrane deformation leads to ____ parasite replication | reduced |
| Host Genetics and Resistance to Malaria is a ____ advantage | heterozygote |
| Proteins related in ____ and ____. | primary amino acid sequence and 3D structure |
| protein families are | homologous |
| oxygen carriers in vertebrates. O2 is bound to a non-protein group termed Heme. Heme enables hemoglobin to pick up O2 from the lungs and release it in tissue. Heme gives blood its red color." | hemoglobin and myglobin |
| - In red blood cells. CO2 and H+ are allosteric effectors. They bind at sites distal from the O2 binding site and promote the release of bound O2. | hemoglobin |
| located in muscle and provides a reserve supply of oxygen. | myoglobin |
| ____ is not an allosteric protein | myoglobin |
| myoglobin and leghemoglobin have tertiary structure similar to that of the __ and __ globin | alpha, beta |
| % similarity between myoglobin and a-globin | 25% |
| Separated by speciation event, e.g. α-globin | ortholog |
| duplication within a genome, e.g. α/β-globin, globin/myoglobin | paralog |
| derived from a common ancestor | homolog |
| Part of the polypeptide chain that can fold independently into a compact stable structure | structural domains |
| the number of amino acids of structural domains | 100 |
| Large proteins may have many domains | true |
| is a protease that is injected into a heart attack victim to dissolve blood clots. | TPA (tissue plasminogen activator) |
| Globular • Rod/Stalk • Acidic • Basic • Helix-turn-helix • Greek key, are examples of which kind of protein domains | structural |
| Membrane spanning • DNA binding • Nucleotide binding • Kinase, are examples of which kind of protein domains | functional |
| region where two different polypeptides interact | Dimerization region |
| region that interacts with another molecule (ligand) through non-covalent interactions | binding site |
| region where catalysis takes place on enzyme | active site |
| binding site for molecule which affects activity of protein (frequently through conformational changes). | regulatory site |
| Small domains also referred to as motifs, e.g. Zinc Finger (DNA-binding domain) | structural motifs |
| Many proteins have multiple domains, each with similar functions | false |
| cAMP binding domain and DNA binding domain, regulatory transcription factor. | catabolite activator protein (CAP) |
| Leucine every 7th AA | leucine zipper |
| hydrophobic interactions between amino acids (leucine) result in helical structure known as | coiled coil |
| CAP binds to DNA as a ___: two polypeptides held together by a coiled-coil interaction | dimer |
| zippers must be homodimers | false |
| Extracellular proteins are frequently stabilized by ____ linkages | covalent |
| Cytosolic proteins are exposed to ____ concentrations of reducing agents and are not found covalently linked | high, |
| • removal of peptide segments • commonly seen in proteins that are activated in response to specific conditions (hormones) or in specific locations (proteases) | processing |
| Acetyl group can be added to the N- or the C-termini or internal N-lysyl groups {Ch3- co- } | acetylation |
| type of protein commonly acetylated | histones |
| Proteins are frequently modified covalently after their synthesis. | true |
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